フォールディング (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "フォールディング" in Japanese language version.

refsWebsite

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85nih.gov

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66doi.org

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24harvard.edu

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1sciencemag.org

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1mit.edu

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1nature.com

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1proteinstructures.com

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1biomolecular-modeling.com

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archive.org

Pratt, Charlotte; Cornely, Kathleen (2004). “Thermodynamics”. Essential Biochemistry. Wiley. ISBN 978-0-471-39387-0 2016年11月26日閲覧。

arxiv.org

Irbäck, Anders; Sandelin, Erik (November 2000). “On Hydrophobicity Correlations in Protein Chains”. Biophysical Journal 79 (5): 2252–2258. arXiv:cond-mat/0010390. Bibcode: 2000BpJ....79.2252I. doi:10.1016/S0006-3495(00)76472-1. PMC 1301114. PMID 11053106.
Irbäck, A.; Peterson, C.; Potthast, F. (3 September 1996). “Evidence for nonrandom hydrophobicity structures in protein chains.”. Proceedings of the National Academy of Sciences 93 (18): 9533–9538. arXiv:chem-ph/9512004. Bibcode: 1996PNAS...93.9533I. doi:10.1073/pnas.93.18.9533. PMC 38463. PMID 8790365.
Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (March 1995). “Funnels, pathways, and the energy landscape of protein folding: a synthesis”. Proteins 21 (3): 167–95. arXiv:chem-ph/9411008. doi:10.1002/prot.340210302. PMID 7784423.

biomolecular-modeling.com

“Protein folding” (by Molecular Dynamics). 2020年10月12日閲覧。

books.google.com

bu.edu

people.bu.edu

Cowtan K (2001). "Phase Problem in X-ray Crystallography, and Its Solution" (PDF). Encyclopedia of Life Sciences. Macmillan Publishers Ltd, Nature Publishing Group. 2016年11月3日閲覧。

doi.org

“So much more to know”. Science 309 (5731): 78–102. (July 2005). doi:10.1126/science.309.5731.78b. PMID 15994524.
Dill KA (June 2008). “The Protein Folding Problem”. Annu Rev Biophys 37: 289–316. doi:10.1146/annurev.biophys.37.092707.153558. PMC 2443096. PMID 18573083.
Anfinsen CB (July 1972). “The formation and stabilization of protein structure”. The Biochemical Journal 128 (4): 737–49. doi:10.1042/bj1280737. PMC 1173893. PMID 4565129.
Selkoe DJ (December 2003). “Folding proteins in fatal ways”. Nature 426 (6968): 900–4. Bibcode: 2003Natur.426..900S. doi:10.1038/nature02264. PMID 14685251.
Kim PS, Baldwin RL (1990). “Intermediates in the folding reactions of small proteins”. Annual Review of Biochemistry 59: 631–60. doi:10.1146/annurev.bi.59.070190.003215. PMID 2197986.
Jackson SE (1998). “How do small single-domain proteins fold?”. Folding & Design 3 (4): R81-91. doi:10.1016/S1359-0278(98)00033-9. PMID 9710577.
Kubelka J, Hofrichter J, Eaton WA (February 2004). “The protein folding 'speed limit'”. Current Opinion in Structural Biology 14 (1): 76–88. doi:10.1016/j.sbi.2004.01.013. PMID 15102453. https://zenodo.org/record/1259347.
Anfinsen CB (July 1973). “Principles that govern the folding of protein chains”. Science 181 (4096): 223–30. Bibcode: 1973Sci...181..223A. doi:10.1126/science.181.4096.223. PMID 4124164.
Alexander PA, He Y, Chen Y, Orban J, Bryan PN (July 2007). “The design and characterization of two proteins with 88% sequence identity but different structure and function”. Proceedings of the National Academy of Sciences of the United States of America 104 (29): 11963–8. Bibcode: 2007PNAS..10411963A. doi:10.1073/pnas.0700922104. PMC 1906725. PMID 17609385.
Rose GD, Fleming PJ, Banavar JR, Maritan A (November 2006). “A backbone-based theory of protein folding”. Proceedings of the National Academy of Sciences of the United States of America 103 (45): 16623–33. Bibcode: 2006PNAS..10316623R. doi:10.1073/pnas.0606843103. PMC 1636505. PMID 17075053.
Fedorov AN (1997). “Cotranslational Protein Folding”. J. Biol. Chem. 272 (52): 32715-32718. doi:10.1074/jbc.272.52.32715.
Zhang, Gong; Ignatova, Zoya (2011-02-01). “Folding at the birth of the nascent chain: coordinating translation with co-translational folding”. Current Opinion in Structural Biology 21 (1): 25–31. doi:10.1016/j.sbi.2010.10.008. ISSN 0959-440X. PMID 21111607.
van den Berg B, Wain R, Dobson CM, Ellis RJ (August 2000). “Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell”. The EMBO Journal 19 (15): 3870–5. doi:10.1093/emboj/19.15.3870. PMC 306593. PMID 10921869.
Pace CN, Shirley BA, McNutt M, Gajiwala K (January 1996). “Forces contributing to the conformational stability of proteins”. FASEB Journal 10 (1): 75–83. doi:10.1096/fasebj.10.1.8566551. PMID 8566551.
Cui D, Ou S, Patel S (December 2014). “Protein-spanning water networks and implications for prediction of protein-protein interactions mediated through hydrophobic effects”. Proteins 82 (12): 3312–26. doi:10.1002/prot.24683. PMID 25204743.
Tanford C (June 1978). “The hydrophobic effect and the organization of living matter”. Science 200 (4345): 1012–8. Bibcode: 1978Sci...200.1012T. doi:10.1126/science.653353. PMID 653353.
Deechongkit S, Nguyen H, Powers ET, Dawson PE, Gruebele M, Kelly JW (July 2004). “Context-dependent contributions of backbone hydrogen bonding to beta-sheet folding energetics”. Nature 430 (6995): 101–5. Bibcode: 2004Natur.430..101D. doi:10.1038/nature02611. PMID 15229605.
Irbäck, Anders; Sandelin, Erik (November 2000). “On Hydrophobicity Correlations in Protein Chains”. Biophysical Journal 79 (5): 2252–2258. arXiv:cond-mat/0010390. Bibcode: 2000BpJ....79.2252I. doi:10.1016/S0006-3495(00)76472-1. PMC 1301114. PMID 11053106.
Irbäck, A.; Peterson, C.; Potthast, F. (3 September 1996). “Evidence for nonrandom hydrophobicity structures in protein chains.”. Proceedings of the National Academy of Sciences 93 (18): 9533–9538. arXiv:chem-ph/9512004. Bibcode: 1996PNAS...93.9533I. doi:10.1073/pnas.93.18.9533. PMC 38463. PMID 8790365.
Wilson, Benjamin A.; Foy, Scott G.; Neme, Rafik; Masel, Joanna (24 April 2017). “Young genes are highly disordered as predicted by the preadaptation hypothesis of de novo gene birth”. Nature Ecology & Evolution 1 (6): 0146–146. doi:10.1038/s41559-017-0146. PMC 5476217. PMID 28642936.
Willis, Sara; Masel, Joanna (September 2018). “Gene Birth Contributes to Structural Disorder Encoded by Overlapping Genes”. Genetics 210 (1): 303–313. doi:10.1534/genetics.118.301249. PMC 6116962. PMID 30026186.
Foy, Scott G.; Wilson, Benjamin A.; Bertram, Jason; Cordes, Matthew H. J.; Masel, Joanna (April 2019). “A Shift in Aggregation Avoidance Strategy Marks a Long-Term Direction to Protein Evolution”. Genetics 211 (4): 1345–1355. doi:10.1534/genetics.118.301719. PMC 6456324. PMID 30692195.
Dobson CM (December 2003). “Protein folding and misfolding”. Nature 426 (6968): 884–90. Bibcode: 2003Natur.426..884D. doi:10.1038/nature02261. PMID 14685248.
Hartl FU (June 1996). “Molecular chaperones in cellular protein folding”. Nature 381 (6583): 571–9. Bibcode: 1996Natur.381..571H. doi:10.1038/381571a0. PMID 8637592.
Hartl FU, Bracher A, Hayer-Hartl M (July 2011). “Molecular chaperones in protein folding and proteostasis”. Nature 475 (7356): 324–32. doi:10.1038/nature10317. PMID 21776078.
Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU (2013). “Molecular chaperone functions in protein folding and proteostasis”. Annual Review of Biochemistry 82: 323–55. doi:10.1146/annurev-biochem-060208-092442. PMID 23746257.
Shortle D (January 1996). “The denatured state (the other half of the folding equation) and its role in protein stability”. FASEB Journal 10 (1): 27–34. doi:10.1096/fasebj.10.1.8566543. PMID 8566543.
Lee S, Tsai FT (2005). “Molecular chaperones in protein quality control”. Journal of Biochemistry and Molecular Biology 38 (3): 259–65. doi:10.5483/BMBRep.2005.38.3.259. PMID 15943899.
Ojeda-May P, Garcia ME (July 2010). “Electric field-driven disruption of a native beta-sheet protein conformation and generation of a helix-structure”. Biophysical Journal 99 (2): 595–9. Bibcode: 2010BpJ....99..595O. doi:10.1016/j.bpj.2010.04.040. PMC 2905109. PMID 20643079.
van den Berg B, Ellis RJ, Dobson CM (December 1999). “Effects of macromolecular crowding on protein folding and aggregation”. The EMBO Journal 18 (24): 6927–33. doi:10.1093/emboj/18.24.6927. PMC 1171756. PMID 10601015.
Ellis RJ (July 2006). “Molecular chaperones: assisting assembly in addition to folding”. Trends in Biochemical Sciences 31 (7): 395–401. doi:10.1016/j.tibs.2006.05.001. PMID 16716593.
Takai K, Nakamura K, Toki T, Tsunogai U, Miyazaki M, Miyazaki J, Hirayama H, Nakagawa S, Nunoura T, Horikoshi K (August 2008). “Cell proliferation at 122 degrees C and isotopically heavy CH4 production by a hyperthermophilic methanogen under high-pressure cultivation”. Proceedings of the National Academy of Sciences of the United States of America 105 (31): 10949–54. Bibcode: 2008PNAS..10510949T. doi:10.1073/pnas.0712334105. PMC 2490668. PMID 18664583.
Chaudhuri TK, Paul S (April 2006). “Protein-misfolding diseases and chaperone-based therapeutic approaches”. The FEBS Journal 273 (7): 1331–49. doi:10.1111/j.1742-4658.2006.05181.x. PMID 16689923.
Soto C, Estrada L, Castilla J (March 2006). “Amyloids, prions and the inherent infectious nature of misfolded protein aggregates”. Trends in Biochemical Sciences 31 (3): 150–5. doi:10.1016/j.tibs.2006.01.002. PMID 16473510.
Hammarström P, Wiseman RL, Powers ET, Kelly JW (January 2003). “Prevention of transthyretin amyloid disease by changing protein misfolding energetics”. Science 299 (5607): 713–6. Bibcode: 2003Sci...299..713H. doi:10.1126/science.1079589. PMID 12560553.
Chiti F, Dobson CM (2006). “Protein misfolding, functional amyloid, and human disease”. Annual Review of Biochemistry 75: 333–66. doi:10.1146/annurev.biochem.75.101304.123901. PMID 16756495.
Johnson SM, Wiseman RL, Sekijima Y, Green NS, Adamski-Werner SL, Kelly JW (December 2005). “Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses”. Accounts of Chemical Research 38 (12): 911–21. doi:10.1021/ar020073i. PMID 16359163.
Taylor, Garry (2003). “The phase problem”. Acta Crystallographica Section D 59 (11): 1881–90. doi:10.1107/S0907444903017815. PMID 14573942.
Bedouelle H (February 2016). “Principles and equations for measuring and interpreting protein stability: From monomer to tetramer”. Biochimie 121: 29–37. doi:10.1016/j.biochi.2015.11.013. PMID 26607240.
Monsellier E, Bedouelle H (September 2005). “Quantitative measurement of protein stability from unfolding equilibria monitored with the fluorescence maximum wavelength”. Protein Engineering, Design & Selection 18 (9): 445–56. doi:10.1093/protein/gzi046. PMID 16087653.
Park YC, Bedouelle H (July 1998). “Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions”. The Journal of Biological Chemistry 273 (29): 18052–9. doi:10.1074/jbc.273.29.18052. PMID 9660761.
Ould-Abeih MB, Petit-Topin I, Zidane N, Baron B, Bedouelle H (June 2012). “Multiple folding states and disorder of ribosomal protein SA, a membrane receptor for laminin, anticarcinogens, and pathogens”. Biochemistry 51 (24): 4807–21. doi:10.1021/bi300335r. PMID 22640394.
Royer CA (May 2006). “Probing protein folding and conformational transitions with fluorescence”. Chemical Reviews 106 (5): 1769–84. doi:10.1021/cr0404390. PMID 16683754.
Cross, Graham H.; Freeman, Neville J.; Swann, Marcus J. (2008). “Dual Polarization Interferometry: A Real-Time Optical Technique for Measuring (Bio)molecular Orientation, Structure and Function at the Solid/Liquid Interface”. Handbook of Biosensors and Biochips. doi:10.1002/9780470061565.hbb055. ISBN 978-0-470-01905-4
Bu Z, Cook J, Callaway DJ (September 2001). “Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin”. Journal of Molecular Biology 312 (4): 865–73. doi:10.1006/jmbi.2001.5006. PMID 11575938.
Minde DP, Maurice MM, Rüdiger SG (2012). “Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp”. PLOS ONE 7 (10): e46147. Bibcode: 2012PLoSO...746147M. doi:10.1371/journal.pone.0046147. PMC 3463568. PMID 23056252.
Park C, Marqusee S (March 2005). “Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding”. Nature Methods 2 (3): 207–12. doi:10.1038/nmeth740. PMID 15782190.
Mashaghi A, Kramer G, Lamb DC, Mayer MP, Tans SJ (January 2014). “Chaperone action at the single-molecule level”. Chemical Reviews 114 (1): 660–76. doi:10.1021/cr400326k. PMID 24001118.
Jagannathan B, Marqusee S (November 2013). “Protein folding and unfolding under force”. Biopolymers 99 (11): 860–9. doi:10.1002/bip.22321. PMC 4065244. PMID 23784721.
Jakobi AJ, Mashaghi A, Tans SJ, Huizinga EG (July 2011). “Calcium modulates force sensing by the von Willebrand factor A2 domain”. Nature Communications 2: 385. Bibcode: 2011NatCo...2..385J. doi:10.1038/ncomms1385. PMC 3144584. PMID 21750539.
Jagannathan B, Elms PJ, Bustamante C, Marqusee S (October 2012). “Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein”. Proceedings of the National Academy of Sciences of the United States of America 109 (44): 17820–5. Bibcode: 2012PNAS..10917820J. doi:10.1073/pnas.1201800109. PMC 3497811. PMID 22949695.
Minde DP, Ramakrishna M, Lilley KS (2018). “Biotinylation by proximity labelling favours unfolded proteins”. bioRxiv. doi:10.1101/274761.
Compiani M, Capriotti E (December 2013). “Computational and theoretical methods for protein folding”. Biochemistry 52 (48): 8601–24. doi:10.1021/bi4001529. PMID 24187909.
Levinthal, Cyrus (1968). “Are there pathways for protein folding?”. Journal de Chimie Physique et de Physico-Chimie Biologique 65: 44–45. Bibcode: 1968JCP....65...44L. doi:10.1051/jcp/1968650044. オリジナルの2009-09-02時点におけるアーカイブ。.
Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (March 1995). “Funnels, pathways, and the energy landscape of protein folding: a synthesis”. Proteins 21 (3): 167–95. arXiv:chem-ph/9411008. doi:10.1002/prot.340210302. PMID 7784423.
Leopold PE; Montal M; Onuchic JN (September 1992). “Protein folding funnels: a kinetic approach to the sequence-structure relationship”. Proceedings of the National Academy of Sciences of the United States of America 89 (18): 8721–5. Bibcode: 1992PNAS...89.8721L. doi:10.1073/pnas.89.18.8721. PMC 49992. PMID 1528885.
Sharma, Vivek; Kaila, Ville R.I.; Annila, Arto (2009). “Protein folding as an evolutionary process”. Physica A: Statistical Mechanics and Its Applications 388 (6): 851–62. Bibcode: 2009PhyA..388..851S. doi:10.1016/j.physa.2008.12.004.
Robson, Barry; Vaithilingam, Andy (2008). “Protein Folding Revisited”. Molecular Biology of Protein Folding, Part B. Progress in Molecular Biology and Translational Science. 84. pp. 161–202. doi:10.1016/S0079-6603(08)00405-4. ISBN 978-0-12-374595-8. PMID 19121702
Dill KA, MacCallum JL (November 2012). “The protein-folding problem, 50 years on”. Science 338 (6110): 1042–6. Bibcode: 2012Sci...338.1042D. doi:10.1126/science.1219021. PMID 23180855.
Fersht AR (February 2000). “Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism”. Proceedings of the National Academy of Sciences of the United States of America 97 (4): 1525–9. Bibcode: 2000PNAS...97.1525F. doi:10.1073/pnas.97.4.1525. PMC 26468. PMID 10677494.
Rizzuti B, Daggett V (March 2013). “Using simulations to provide the framework for experimental protein folding studies”. Archives of Biochemistry and Biophysics 531 (1–2): 128–35. doi:10.1016/j.abb.2012.12.015. PMC 4084838. PMID 23266569.
Schaefer M, Bartels C, Karplus M (December 1998). “Solution conformations and thermodynamics of structured peptides: molecular dynamics simulation with an implicit solvation model”. Journal of Molecular Biology 284 (3): 835–48. doi:10.1006/jmbi.1998.2172. PMID 9826519.
Kmiecik S, Gront D, Kolinski M, Wieteska L, Dawid AE, Kolinski A (July 2016). “Coarse-Grained Protein Models and Their Applications”. Chemical Reviews 116 (14): 7898–936. doi:10.1021/acs.chemrev.6b00163. PMID 27333362.
Kmiecik S, Kolinski A (July 2007). “Characterization of protein-folding pathways by reduced-space modeling”. Proceedings of the National Academy of Sciences of the United States of America 104 (30): 12330–5. Bibcode: 2007PNAS..10412330K. doi:10.1073/pnas.0702265104. PMC 1941469. PMID 17636132.
Adhikari AN, Freed KF, Sosnick TR (October 2012). “De novo prediction of protein folding pathways and structure using the principle of sequential stabilization”. Proceedings of the National Academy of Sciences of the United States of America 109 (43): 17442–7. Bibcode: 2012PNAS..10917442A. doi:10.1073/pnas.1209000109. PMC 3491489. PMID 23045636.
Lindorff-Larsen K, Piana S, Dror RO, Shaw DE (October 2011). “How fast-folding proteins fold”. Science 334 (6055): 517–20. Bibcode: 2011Sci...334..517L. doi:10.1126/science.1208351. PMID 22034434.

harvard.edu

ui.adsabs.harvard.edu

Selkoe DJ (December 2003). “Folding proteins in fatal ways”. Nature 426 (6968): 900–4. Bibcode: 2003Natur.426..900S. doi:10.1038/nature02264. PMID 14685251.
Anfinsen CB (July 1973). “Principles that govern the folding of protein chains”. Science 181 (4096): 223–30. Bibcode: 1973Sci...181..223A. doi:10.1126/science.181.4096.223. PMID 4124164.
Alexander PA, He Y, Chen Y, Orban J, Bryan PN (July 2007). “The design and characterization of two proteins with 88% sequence identity but different structure and function”. Proceedings of the National Academy of Sciences of the United States of America 104 (29): 11963–8. Bibcode: 2007PNAS..10411963A. doi:10.1073/pnas.0700922104. PMC 1906725. PMID 17609385.
Rose GD, Fleming PJ, Banavar JR, Maritan A (November 2006). “A backbone-based theory of protein folding”. Proceedings of the National Academy of Sciences of the United States of America 103 (45): 16623–33. Bibcode: 2006PNAS..10316623R. doi:10.1073/pnas.0606843103. PMC 1636505. PMID 17075053.
Tanford C (June 1978). “The hydrophobic effect and the organization of living matter”. Science 200 (4345): 1012–8. Bibcode: 1978Sci...200.1012T. doi:10.1126/science.653353. PMID 653353.
Deechongkit S, Nguyen H, Powers ET, Dawson PE, Gruebele M, Kelly JW (July 2004). “Context-dependent contributions of backbone hydrogen bonding to beta-sheet folding energetics”. Nature 430 (6995): 101–5. Bibcode: 2004Natur.430..101D. doi:10.1038/nature02611. PMID 15229605.
Irbäck, Anders; Sandelin, Erik (November 2000). “On Hydrophobicity Correlations in Protein Chains”. Biophysical Journal 79 (5): 2252–2258. arXiv:cond-mat/0010390. Bibcode: 2000BpJ....79.2252I. doi:10.1016/S0006-3495(00)76472-1. PMC 1301114. PMID 11053106.
Irbäck, A.; Peterson, C.; Potthast, F. (3 September 1996). “Evidence for nonrandom hydrophobicity structures in protein chains.”. Proceedings of the National Academy of Sciences 93 (18): 9533–9538. arXiv:chem-ph/9512004. Bibcode: 1996PNAS...93.9533I. doi:10.1073/pnas.93.18.9533. PMC 38463. PMID 8790365.
Dobson CM (December 2003). “Protein folding and misfolding”. Nature 426 (6968): 884–90. Bibcode: 2003Natur.426..884D. doi:10.1038/nature02261. PMID 14685248.
Hartl FU (June 1996). “Molecular chaperones in cellular protein folding”. Nature 381 (6583): 571–9. Bibcode: 1996Natur.381..571H. doi:10.1038/381571a0. PMID 8637592.
Ojeda-May P, Garcia ME (July 2010). “Electric field-driven disruption of a native beta-sheet protein conformation and generation of a helix-structure”. Biophysical Journal 99 (2): 595–9. Bibcode: 2010BpJ....99..595O. doi:10.1016/j.bpj.2010.04.040. PMC 2905109. PMID 20643079.
Takai K, Nakamura K, Toki T, Tsunogai U, Miyazaki M, Miyazaki J, Hirayama H, Nakagawa S, Nunoura T, Horikoshi K (August 2008). “Cell proliferation at 122 degrees C and isotopically heavy CH4 production by a hyperthermophilic methanogen under high-pressure cultivation”. Proceedings of the National Academy of Sciences of the United States of America 105 (31): 10949–54. Bibcode: 2008PNAS..10510949T. doi:10.1073/pnas.0712334105. PMC 2490668. PMID 18664583.
Hammarström P, Wiseman RL, Powers ET, Kelly JW (January 2003). “Prevention of transthyretin amyloid disease by changing protein misfolding energetics”. Science 299 (5607): 713–6. Bibcode: 2003Sci...299..713H. doi:10.1126/science.1079589. PMID 12560553.
Minde DP, Maurice MM, Rüdiger SG (2012). “Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp”. PLOS ONE 7 (10): e46147. Bibcode: 2012PLoSO...746147M. doi:10.1371/journal.pone.0046147. PMC 3463568. PMID 23056252.
Jakobi AJ, Mashaghi A, Tans SJ, Huizinga EG (July 2011). “Calcium modulates force sensing by the von Willebrand factor A2 domain”. Nature Communications 2: 385. Bibcode: 2011NatCo...2..385J. doi:10.1038/ncomms1385. PMC 3144584. PMID 21750539.
Jagannathan B, Elms PJ, Bustamante C, Marqusee S (October 2012). “Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein”. Proceedings of the National Academy of Sciences of the United States of America 109 (44): 17820–5. Bibcode: 2012PNAS..10917820J. doi:10.1073/pnas.1201800109. PMC 3497811. PMID 22949695.
Levinthal, Cyrus (1968). “Are there pathways for protein folding?”. Journal de Chimie Physique et de Physico-Chimie Biologique 65: 44–45. Bibcode: 1968JCP....65...44L. doi:10.1051/jcp/1968650044. オリジナルの2009-09-02時点におけるアーカイブ。.
Leopold PE; Montal M; Onuchic JN (September 1992). “Protein folding funnels: a kinetic approach to the sequence-structure relationship”. Proceedings of the National Academy of Sciences of the United States of America 89 (18): 8721–5. Bibcode: 1992PNAS...89.8721L. doi:10.1073/pnas.89.18.8721. PMC 49992. PMID 1528885.
Sharma, Vivek; Kaila, Ville R.I.; Annila, Arto (2009). “Protein folding as an evolutionary process”. Physica A: Statistical Mechanics and Its Applications 388 (6): 851–62. Bibcode: 2009PhyA..388..851S. doi:10.1016/j.physa.2008.12.004.
Dill KA, MacCallum JL (November 2012). “The protein-folding problem, 50 years on”. Science 338 (6110): 1042–6. Bibcode: 2012Sci...338.1042D. doi:10.1126/science.1219021. PMID 23180855.
Fersht AR (February 2000). “Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism”. Proceedings of the National Academy of Sciences of the United States of America 97 (4): 1525–9. Bibcode: 2000PNAS...97.1525F. doi:10.1073/pnas.97.4.1525. PMC 26468. PMID 10677494.
Kmiecik S, Kolinski A (July 2007). “Characterization of protein-folding pathways by reduced-space modeling”. Proceedings of the National Academy of Sciences of the United States of America 104 (30): 12330–5. Bibcode: 2007PNAS..10412330K. doi:10.1073/pnas.0702265104. PMC 1941469. PMID 17636132.
Adhikari AN, Freed KF, Sosnick TR (October 2012). “De novo prediction of protein folding pathways and structure using the principle of sequential stabilization”. Proceedings of the National Academy of Sciences of the United States of America 109 (43): 17442–7. Bibcode: 2012PNAS..10917442A. doi:10.1073/pnas.1209000109. PMC 3491489. PMID 23045636.
Lindorff-Larsen K, Piana S, Dror RO, Shaw DE (October 2011). “How fast-folding proteins fold”. Science 334 (6055): 517–20. Bibcode: 2011Sci...334..517L. doi:10.1126/science.1208351. PMID 22034434.

mit.edu

ocw.mit.edu

King (2007年). “MIT OpenCourseWare - 7.88J / 5.48J / 7.24J / 10.543J Protein Folding Problem, Fall 2007 Lecture Notes - 1”. MIT OpenCourseWare. 2013年9月28日時点のオリジナルよりアーカイブ。2013年6月22日閲覧。

nature.com

“Protein Structure”. Scitable. Nature Education. 2016年11月26日閲覧。

nih.gov

pubmed.ncbi.nlm.nih.gov

“So much more to know”. Science 309 (5731): 78–102. (July 2005). doi:10.1126/science.309.5731.78b. PMID 15994524.
Dill KA (June 2008). “The Protein Folding Problem”. Annu Rev Biophys 37: 289–316. doi:10.1146/annurev.biophys.37.092707.153558. PMC 2443096. PMID 18573083.
Anfinsen CB (July 1972). “The formation and stabilization of protein structure”. The Biochemical Journal 128 (4): 737–49. doi:10.1042/bj1280737. PMC 1173893. PMID 4565129.
Selkoe DJ (December 2003). “Folding proteins in fatal ways”. Nature 426 (6968): 900–4. Bibcode: 2003Natur.426..900S. doi:10.1038/nature02264. PMID 14685251.
Kim PS, Baldwin RL (1990). “Intermediates in the folding reactions of small proteins”. Annual Review of Biochemistry 59: 631–60. doi:10.1146/annurev.bi.59.070190.003215. PMID 2197986.
Jackson SE (1998). “How do small single-domain proteins fold?”. Folding & Design 3 (4): R81-91. doi:10.1016/S1359-0278(98)00033-9. PMID 9710577.
Kubelka J, Hofrichter J, Eaton WA (February 2004). “The protein folding 'speed limit'”. Current Opinion in Structural Biology 14 (1): 76–88. doi:10.1016/j.sbi.2004.01.013. PMID 15102453. https://zenodo.org/record/1259347.
Anfinsen CB (July 1973). “Principles that govern the folding of protein chains”. Science 181 (4096): 223–30. Bibcode: 1973Sci...181..223A. doi:10.1126/science.181.4096.223. PMID 4124164.
Alexander PA, He Y, Chen Y, Orban J, Bryan PN (July 2007). “The design and characterization of two proteins with 88% sequence identity but different structure and function”. Proceedings of the National Academy of Sciences of the United States of America 104 (29): 11963–8. Bibcode: 2007PNAS..10411963A. doi:10.1073/pnas.0700922104. PMC 1906725. PMID 17609385.
Rose GD, Fleming PJ, Banavar JR, Maritan A (November 2006). “A backbone-based theory of protein folding”. Proceedings of the National Academy of Sciences of the United States of America 103 (45): 16623–33. Bibcode: 2006PNAS..10316623R. doi:10.1073/pnas.0606843103. PMC 1636505. PMID 17075053.
Zhang, Gong; Ignatova, Zoya (2011-02-01). “Folding at the birth of the nascent chain: coordinating translation with co-translational folding”. Current Opinion in Structural Biology 21 (1): 25–31. doi:10.1016/j.sbi.2010.10.008. ISSN 0959-440X. PMID 21111607.
van den Berg B, Wain R, Dobson CM, Ellis RJ (August 2000). “Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell”. The EMBO Journal 19 (15): 3870–5. doi:10.1093/emboj/19.15.3870. PMC 306593. PMID 10921869.
Pace CN, Shirley BA, McNutt M, Gajiwala K (January 1996). “Forces contributing to the conformational stability of proteins”. FASEB Journal 10 (1): 75–83. doi:10.1096/fasebj.10.1.8566551. PMID 8566551.
Cui D, Ou S, Patel S (December 2014). “Protein-spanning water networks and implications for prediction of protein-protein interactions mediated through hydrophobic effects”. Proteins 82 (12): 3312–26. doi:10.1002/prot.24683. PMID 25204743.
Tanford C (June 1978). “The hydrophobic effect and the organization of living matter”. Science 200 (4345): 1012–8. Bibcode: 1978Sci...200.1012T. doi:10.1126/science.653353. PMID 653353.
Deechongkit S, Nguyen H, Powers ET, Dawson PE, Gruebele M, Kelly JW (July 2004). “Context-dependent contributions of backbone hydrogen bonding to beta-sheet folding energetics”. Nature 430 (6995): 101–5. Bibcode: 2004Natur.430..101D. doi:10.1038/nature02611. PMID 15229605.
Irbäck, Anders; Sandelin, Erik (November 2000). “On Hydrophobicity Correlations in Protein Chains”. Biophysical Journal 79 (5): 2252–2258. arXiv:cond-mat/0010390. Bibcode: 2000BpJ....79.2252I. doi:10.1016/S0006-3495(00)76472-1. PMC 1301114. PMID 11053106.
Irbäck, A.; Peterson, C.; Potthast, F. (3 September 1996). “Evidence for nonrandom hydrophobicity structures in protein chains.”. Proceedings of the National Academy of Sciences 93 (18): 9533–9538. arXiv:chem-ph/9512004. Bibcode: 1996PNAS...93.9533I. doi:10.1073/pnas.93.18.9533. PMC 38463. PMID 8790365.
Wilson, Benjamin A.; Foy, Scott G.; Neme, Rafik; Masel, Joanna (24 April 2017). “Young genes are highly disordered as predicted by the preadaptation hypothesis of de novo gene birth”. Nature Ecology & Evolution 1 (6): 0146–146. doi:10.1038/s41559-017-0146. PMC 5476217. PMID 28642936.
Willis, Sara; Masel, Joanna (September 2018). “Gene Birth Contributes to Structural Disorder Encoded by Overlapping Genes”. Genetics 210 (1): 303–313. doi:10.1534/genetics.118.301249. PMC 6116962. PMID 30026186.
Foy, Scott G.; Wilson, Benjamin A.; Bertram, Jason; Cordes, Matthew H. J.; Masel, Joanna (April 2019). “A Shift in Aggregation Avoidance Strategy Marks a Long-Term Direction to Protein Evolution”. Genetics 211 (4): 1345–1355. doi:10.1534/genetics.118.301719. PMC 6456324. PMID 30692195.
Dobson CM (December 2003). “Protein folding and misfolding”. Nature 426 (6968): 884–90. Bibcode: 2003Natur.426..884D. doi:10.1038/nature02261. PMID 14685248.
Hartl FU (June 1996). “Molecular chaperones in cellular protein folding”. Nature 381 (6583): 571–9. Bibcode: 1996Natur.381..571H. doi:10.1038/381571a0. PMID 8637592.
Hartl FU, Bracher A, Hayer-Hartl M (July 2011). “Molecular chaperones in protein folding and proteostasis”. Nature 475 (7356): 324–32. doi:10.1038/nature10317. PMID 21776078.
Kim YE, Hipp MS, Bracher A, Hayer-Hartl M, Hartl FU (2013). “Molecular chaperone functions in protein folding and proteostasis”. Annual Review of Biochemistry 82: 323–55. doi:10.1146/annurev-biochem-060208-092442. PMID 23746257.
Shortle D (January 1996). “The denatured state (the other half of the folding equation) and its role in protein stability”. FASEB Journal 10 (1): 27–34. doi:10.1096/fasebj.10.1.8566543. PMID 8566543.
Lee S, Tsai FT (2005). “Molecular chaperones in protein quality control”. Journal of Biochemistry and Molecular Biology 38 (3): 259–65. doi:10.5483/BMBRep.2005.38.3.259. PMID 15943899.
Ojeda-May P, Garcia ME (July 2010). “Electric field-driven disruption of a native beta-sheet protein conformation and generation of a helix-structure”. Biophysical Journal 99 (2): 595–9. Bibcode: 2010BpJ....99..595O. doi:10.1016/j.bpj.2010.04.040. PMC 2905109. PMID 20643079.
van den Berg B, Ellis RJ, Dobson CM (December 1999). “Effects of macromolecular crowding on protein folding and aggregation”. The EMBO Journal 18 (24): 6927–33. doi:10.1093/emboj/18.24.6927. PMC 1171756. PMID 10601015.
Ellis RJ (July 2006). “Molecular chaperones: assisting assembly in addition to folding”. Trends in Biochemical Sciences 31 (7): 395–401. doi:10.1016/j.tibs.2006.05.001. PMID 16716593.
Takai K, Nakamura K, Toki T, Tsunogai U, Miyazaki M, Miyazaki J, Hirayama H, Nakagawa S, Nunoura T, Horikoshi K (August 2008). “Cell proliferation at 122 degrees C and isotopically heavy CH4 production by a hyperthermophilic methanogen under high-pressure cultivation”. Proceedings of the National Academy of Sciences of the United States of America 105 (31): 10949–54. Bibcode: 2008PNAS..10510949T. doi:10.1073/pnas.0712334105. PMC 2490668. PMID 18664583.
Chaudhuri TK, Paul S (April 2006). “Protein-misfolding diseases and chaperone-based therapeutic approaches”. The FEBS Journal 273 (7): 1331–49. doi:10.1111/j.1742-4658.2006.05181.x. PMID 16689923.
Soto C, Estrada L, Castilla J (March 2006). “Amyloids, prions and the inherent infectious nature of misfolded protein aggregates”. Trends in Biochemical Sciences 31 (3): 150–5. doi:10.1016/j.tibs.2006.01.002. PMID 16473510.
Hammarström P, Wiseman RL, Powers ET, Kelly JW (January 2003). “Prevention of transthyretin amyloid disease by changing protein misfolding energetics”. Science 299 (5607): 713–6. Bibcode: 2003Sci...299..713H. doi:10.1126/science.1079589. PMID 12560553.
Chiti F, Dobson CM (2006). “Protein misfolding, functional amyloid, and human disease”. Annual Review of Biochemistry 75: 333–66. doi:10.1146/annurev.biochem.75.101304.123901. PMID 16756495.
Johnson SM, Wiseman RL, Sekijima Y, Green NS, Adamski-Werner SL, Kelly JW (December 2005). “Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: a focus on the transthyretin amyloidoses”. Accounts of Chemical Research 38 (12): 911–21. doi:10.1021/ar020073i. PMID 16359163.
Taylor, Garry (2003). “The phase problem”. Acta Crystallographica Section D 59 (11): 1881–90. doi:10.1107/S0907444903017815. PMID 14573942.
Bedouelle H (February 2016). “Principles and equations for measuring and interpreting protein stability: From monomer to tetramer”. Biochimie 121: 29–37. doi:10.1016/j.biochi.2015.11.013. PMID 26607240.
Monsellier E, Bedouelle H (September 2005). “Quantitative measurement of protein stability from unfolding equilibria monitored with the fluorescence maximum wavelength”. Protein Engineering, Design & Selection 18 (9): 445–56. doi:10.1093/protein/gzi046. PMID 16087653.
Park YC, Bedouelle H (July 1998). “Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions”. The Journal of Biological Chemistry 273 (29): 18052–9. doi:10.1074/jbc.273.29.18052. PMID 9660761.
Ould-Abeih MB, Petit-Topin I, Zidane N, Baron B, Bedouelle H (June 2012). “Multiple folding states and disorder of ribosomal protein SA, a membrane receptor for laminin, anticarcinogens, and pathogens”. Biochemistry 51 (24): 4807–21. doi:10.1021/bi300335r. PMID 22640394.
Royer CA (May 2006). “Probing protein folding and conformational transitions with fluorescence”. Chemical Reviews 106 (5): 1769–84. doi:10.1021/cr0404390. PMID 16683754.
Bu Z, Cook J, Callaway DJ (September 2001). “Dynamic regimes and correlated structural dynamics in native and denatured alpha-lactalbumin”. Journal of Molecular Biology 312 (4): 865–73. doi:10.1006/jmbi.2001.5006. PMID 11575938.
Minde DP, Maurice MM, Rüdiger SG (2012). “Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp”. PLOS ONE 7 (10): e46147. Bibcode: 2012PLoSO...746147M. doi:10.1371/journal.pone.0046147. PMC 3463568. PMID 23056252.
Park C, Marqusee S (March 2005). “Pulse proteolysis: a simple method for quantitative determination of protein stability and ligand binding”. Nature Methods 2 (3): 207–12. doi:10.1038/nmeth740. PMID 15782190.
Mashaghi A, Kramer G, Lamb DC, Mayer MP, Tans SJ (January 2014). “Chaperone action at the single-molecule level”. Chemical Reviews 114 (1): 660–76. doi:10.1021/cr400326k. PMID 24001118.
Jagannathan B, Marqusee S (November 2013). “Protein folding and unfolding under force”. Biopolymers 99 (11): 860–9. doi:10.1002/bip.22321. PMC 4065244. PMID 23784721.
Jakobi AJ, Mashaghi A, Tans SJ, Huizinga EG (July 2011). “Calcium modulates force sensing by the von Willebrand factor A2 domain”. Nature Communications 2: 385. Bibcode: 2011NatCo...2..385J. doi:10.1038/ncomms1385. PMC 3144584. PMID 21750539.
Jagannathan B, Elms PJ, Bustamante C, Marqusee S (October 2012). “Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein”. Proceedings of the National Academy of Sciences of the United States of America 109 (44): 17820–5. Bibcode: 2012PNAS..10917820J. doi:10.1073/pnas.1201800109. PMC 3497811. PMID 22949695.
Compiani M, Capriotti E (December 2013). “Computational and theoretical methods for protein folding”. Biochemistry 52 (48): 8601–24. doi:10.1021/bi4001529. PMID 24187909.
Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (March 1995). “Funnels, pathways, and the energy landscape of protein folding: a synthesis”. Proteins 21 (3): 167–95. arXiv:chem-ph/9411008. doi:10.1002/prot.340210302. PMID 7784423.
Leopold PE; Montal M; Onuchic JN (September 1992). “Protein folding funnels: a kinetic approach to the sequence-structure relationship”. Proceedings of the National Academy of Sciences of the United States of America 89 (18): 8721–5. Bibcode: 1992PNAS...89.8721L. doi:10.1073/pnas.89.18.8721. PMC 49992. PMID 1528885.
Robson, Barry; Vaithilingam, Andy (2008). “Protein Folding Revisited”. Molecular Biology of Protein Folding, Part B. Progress in Molecular Biology and Translational Science. 84. pp. 161–202. doi:10.1016/S0079-6603(08)00405-4. ISBN 978-0-12-374595-8. PMID 19121702
Dill KA, MacCallum JL (November 2012). “The protein-folding problem, 50 years on”. Science 338 (6110): 1042–6. Bibcode: 2012Sci...338.1042D. doi:10.1126/science.1219021. PMID 23180855.
Fersht AR (February 2000). “Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism”. Proceedings of the National Academy of Sciences of the United States of America 97 (4): 1525–9. Bibcode: 2000PNAS...97.1525F. doi:10.1073/pnas.97.4.1525. PMC 26468. PMID 10677494.
Rizzuti B, Daggett V (March 2013). “Using simulations to provide the framework for experimental protein folding studies”. Archives of Biochemistry and Biophysics 531 (1–2): 128–35. doi:10.1016/j.abb.2012.12.015. PMC 4084838. PMID 23266569.
Schaefer M, Bartels C, Karplus M (December 1998). “Solution conformations and thermodynamics of structured peptides: molecular dynamics simulation with an implicit solvation model”. Journal of Molecular Biology 284 (3): 835–48. doi:10.1006/jmbi.1998.2172. PMID 9826519.
Kmiecik S, Gront D, Kolinski M, Wieteska L, Dawid AE, Kolinski A (July 2016). “Coarse-Grained Protein Models and Their Applications”. Chemical Reviews 116 (14): 7898–936. doi:10.1021/acs.chemrev.6b00163. PMID 27333362.
Kmiecik S, Kolinski A (July 2007). “Characterization of protein-folding pathways by reduced-space modeling”. Proceedings of the National Academy of Sciences of the United States of America 104 (30): 12330–5. Bibcode: 2007PNAS..10412330K. doi:10.1073/pnas.0702265104. PMC 1941469. PMID 17636132.
Adhikari AN, Freed KF, Sosnick TR (October 2012). “De novo prediction of protein folding pathways and structure using the principle of sequential stabilization”. Proceedings of the National Academy of Sciences of the United States of America 109 (43): 17442–7. Bibcode: 2012PNAS..10917442A. doi:10.1073/pnas.1209000109. PMC 3491489. PMID 23045636.
Lindorff-Larsen K, Piana S, Dror RO, Shaw DE (October 2011). “How fast-folding proteins fold”. Science 334 (6055): 517–20. Bibcode: 2011Sci...334..517L. doi:10.1126/science.1208351. PMID 22034434.

ncbi.nlm.nih.gov

Dill KA (June 2008). “The Protein Folding Problem”. Annu Rev Biophys 37: 289–316. doi:10.1146/annurev.biophys.37.092707.153558. PMC 2443096. PMID 18573083.
Alberts, Bruce; Johnson, Alexander; Lewis, Julian; Raff, Martin; Roberts, Keith; Walters, Peter (2002). “The Shape and Structure of Proteins”. Molecular Biology of the Cell; Fourth Edition. New York and London: Garland Science. ISBN 978-0-8153-3218-3
Anfinsen CB (July 1972). “The formation and stabilization of protein structure”. The Biochemical Journal 128 (4): 737–49. doi:10.1042/bj1280737. PMC 1173893. PMID 4565129.
Berg, Jeremy M.; Tymoczko, John L.; Stryer, Lubert (2002). “3. Protein Structure and Function”. Biochemistry. San Francisco: W. H. Freeman. ISBN 978-0-7167-4684-3
Alexander PA, He Y, Chen Y, Orban J, Bryan PN (July 2007). “The design and characterization of two proteins with 88% sequence identity but different structure and function”. Proceedings of the National Academy of Sciences of the United States of America 104 (29): 11963–8. Bibcode: 2007PNAS..10411963A. doi:10.1073/pnas.0700922104. PMC 1906725. PMID 17609385.
Rose GD, Fleming PJ, Banavar JR, Maritan A (November 2006). “A backbone-based theory of protein folding”. Proceedings of the National Academy of Sciences of the United States of America 103 (45): 16623–33. Bibcode: 2006PNAS..10316623R. doi:10.1073/pnas.0606843103. PMC 1636505. PMID 17075053.
van den Berg B, Wain R, Dobson CM, Ellis RJ (August 2000). “Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell”. The EMBO Journal 19 (15): 3870–5. doi:10.1093/emboj/19.15.3870. PMC 306593. PMID 10921869.
Irbäck, Anders; Sandelin, Erik (November 2000). “On Hydrophobicity Correlations in Protein Chains”. Biophysical Journal 79 (5): 2252–2258. arXiv:cond-mat/0010390. Bibcode: 2000BpJ....79.2252I. doi:10.1016/S0006-3495(00)76472-1. PMC 1301114. PMID 11053106.
Irbäck, A.; Peterson, C.; Potthast, F. (3 September 1996). “Evidence for nonrandom hydrophobicity structures in protein chains.”. Proceedings of the National Academy of Sciences 93 (18): 9533–9538. arXiv:chem-ph/9512004. Bibcode: 1996PNAS...93.9533I. doi:10.1073/pnas.93.18.9533. PMC 38463. PMID 8790365.
Wilson, Benjamin A.; Foy, Scott G.; Neme, Rafik; Masel, Joanna (24 April 2017). “Young genes are highly disordered as predicted by the preadaptation hypothesis of de novo gene birth”. Nature Ecology & Evolution 1 (6): 0146–146. doi:10.1038/s41559-017-0146. PMC 5476217. PMID 28642936.
Willis, Sara; Masel, Joanna (September 2018). “Gene Birth Contributes to Structural Disorder Encoded by Overlapping Genes”. Genetics 210 (1): 303–313. doi:10.1534/genetics.118.301249. PMC 6116962. PMID 30026186.
Foy, Scott G.; Wilson, Benjamin A.; Bertram, Jason; Cordes, Matthew H. J.; Masel, Joanna (April 2019). “A Shift in Aggregation Avoidance Strategy Marks a Long-Term Direction to Protein Evolution”. Genetics 211 (4): 1345–1355. doi:10.1534/genetics.118.301719. PMC 6456324. PMID 30692195.
Ojeda-May P, Garcia ME (July 2010). “Electric field-driven disruption of a native beta-sheet protein conformation and generation of a helix-structure”. Biophysical Journal 99 (2): 595–9. Bibcode: 2010BpJ....99..595O. doi:10.1016/j.bpj.2010.04.040. PMC 2905109. PMID 20643079.
van den Berg B, Ellis RJ, Dobson CM (December 1999). “Effects of macromolecular crowding on protein folding and aggregation”. The EMBO Journal 18 (24): 6927–33. doi:10.1093/emboj/18.24.6927. PMC 1171756. PMID 10601015.
Takai K, Nakamura K, Toki T, Tsunogai U, Miyazaki M, Miyazaki J, Hirayama H, Nakagawa S, Nunoura T, Horikoshi K (August 2008). “Cell proliferation at 122 degrees C and isotopically heavy CH4 production by a hyperthermophilic methanogen under high-pressure cultivation”. Proceedings of the National Academy of Sciences of the United States of America 105 (31): 10949–54. Bibcode: 2008PNAS..10510949T. doi:10.1073/pnas.0712334105. PMC 2490668. PMID 18664583.
Minde DP, Maurice MM, Rüdiger SG (2012). “Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp”. PLOS ONE 7 (10): e46147. Bibcode: 2012PLoSO...746147M. doi:10.1371/journal.pone.0046147. PMC 3463568. PMID 23056252.
Jagannathan B, Marqusee S (November 2013). “Protein folding and unfolding under force”. Biopolymers 99 (11): 860–9. doi:10.1002/bip.22321. PMC 4065244. PMID 23784721.
Jakobi AJ, Mashaghi A, Tans SJ, Huizinga EG (July 2011). “Calcium modulates force sensing by the von Willebrand factor A2 domain”. Nature Communications 2: 385. Bibcode: 2011NatCo...2..385J. doi:10.1038/ncomms1385. PMC 3144584. PMID 21750539.
Jagannathan B, Elms PJ, Bustamante C, Marqusee S (October 2012). “Direct observation of a force-induced switch in the anisotropic mechanical unfolding pathway of a protein”. Proceedings of the National Academy of Sciences of the United States of America 109 (44): 17820–5. Bibcode: 2012PNAS..10917820J. doi:10.1073/pnas.1201800109. PMC 3497811. PMID 22949695.
Leopold PE; Montal M; Onuchic JN (September 1992). “Protein folding funnels: a kinetic approach to the sequence-structure relationship”. Proceedings of the National Academy of Sciences of the United States of America 89 (18): 8721–5. Bibcode: 1992PNAS...89.8721L. doi:10.1073/pnas.89.18.8721. PMC 49992. PMID 1528885.
Fersht AR (February 2000). “Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism”. Proceedings of the National Academy of Sciences of the United States of America 97 (4): 1525–9. Bibcode: 2000PNAS...97.1525F. doi:10.1073/pnas.97.4.1525. PMC 26468. PMID 10677494.
Rizzuti B, Daggett V (March 2013). “Using simulations to provide the framework for experimental protein folding studies”. Archives of Biochemistry and Biophysics 531 (1–2): 128–35. doi:10.1016/j.abb.2012.12.015. PMC 4084838. PMID 23266569.
Kmiecik S, Kolinski A (July 2007). “Characterization of protein-folding pathways by reduced-space modeling”. Proceedings of the National Academy of Sciences of the United States of America 104 (30): 12330–5. Bibcode: 2007PNAS..10412330K. doi:10.1073/pnas.0702265104. PMC 1941469. PMID 17636132.
Adhikari AN, Freed KF, Sosnick TR (October 2012). “De novo prediction of protein folding pathways and structure using the principle of sequential stabilization”. Proceedings of the National Academy of Sciences of the United States of America 109 (43): 17442–7. Bibcode: 2012PNAS..10917442A. doi:10.1073/pnas.1209000109. PMC 3491489. PMID 23045636.

proteinstructures.com

Al-Karadaghi, Salam. “Torsion Angles and the Ramachnadran Plot in Protein Structures”. www.proteinstructures.com. 2016年11月26日閲覧。

sciencemag.org

“So much more to know”. Science 309 (5731): 78–102. (July 2005). doi:10.1126/science.309.5731.78b. PMID 15994524.

ucl.ac.uk

cs.ucl.ac.uk

Jones, David. “Fragment-based Protein Folding Simulations”. University College London. 2020年10月12日閲覧。

web.archive.org

King (2007年). “MIT OpenCourseWare - 7.88J / 5.48J / 7.24J / 10.543J Protein Folding Problem, Fall 2007 Lecture Notes - 1”. MIT OpenCourseWare. 2013年9月28日時点のオリジナルよりアーカイブ。2013年6月22日閲覧。
Levinthal, Cyrus (1968). “Are there pathways for protein folding?”. Journal de Chimie Physique et de Physico-Chimie Biologique 65: 44–45. Bibcode: 1968JCP....65...44L. doi:10.1051/jcp/1968650044. オリジナルの2009-09-02時点におけるアーカイブ。.

wikibooks.org

en.wikibooks.org

“Structural Biochemistry/Proteins/Protein Folding - Wikibooks, open books for an open world”. en.wikibooks.org. 2016年11月5日閲覧。

wiley.com

Pratt, Charlotte; Cornely, Kathleen (2004). “Thermodynamics”. Essential Biochemistry. Wiley. ISBN 978-0-471-39387-0 2016年11月26日閲覧。

wisc.edu

biochem.wisc.edu

Levinthal, Cyrus (1968). “Are there pathways for protein folding?”. Journal de Chimie Physique et de Physico-Chimie Biologique 65: 44–45. Bibcode: 1968JCP....65...44L. doi:10.1051/jcp/1968650044. オリジナルの2009-09-02時点におけるアーカイブ。.

worldcat.org

search.worldcat.org

Zhang, Gong; Ignatova, Zoya (2011-02-01). “Folding at the birth of the nascent chain: coordinating translation with co-translational folding”. Current Opinion in Structural Biology 21 (1): 25–31. doi:10.1016/j.sbi.2010.10.008. ISSN 0959-440X. PMID 21111607.

zenodo.org

Kubelka J, Hofrichter J, Eaton WA (February 2004). “The protein folding 'speed limit'”. Current Opinion in Structural Biology 14 (1): 76–88. doi:10.1016/j.sbi.2004.01.013. PMID 15102453. https://zenodo.org/record/1259347.