Δευτεροταγής δομή πρωτεΐνης (Greek Wikipedia)

Analysis of information sources in references of the Wikipedia article "Δευτεροταγής δομή πρωτεΐνης" in Greek language version.

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36nih.gov

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26doi.org

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3archive.org

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1amazon.com

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1curtin.edu.au

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1worldcat.org

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1ucdavis.edu

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1monash.edu.au

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1swmed.edu

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amazon.com

Linderstrøm-Lang KU (1952). Lane Medical Lectures: Proteins and Enzymes. Stanford University Press. σελ. 115. ASIN B0007J31SC.

archive.org

«Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features». Biopolymers 22 (12): 2577–637. Dec 1983. doi:10.1002/bip.360221211. PMID 6667333. https://archive.org/details/sim_biopolymers_1983-12_22_12/page/2577.
«Empirical predictions of protein conformation». Annual Review of Biochemistry 47: 251–76. 1978. doi:10.1146/annurev.bi.47.070178.001343. PMID 354496. https://archive.org/details/sim_annual-review-of-biochemistry_1978_47/page/251.
Chou PY, Fasman GD (1978). «Prediction of the secondary structure of proteins from their amino acid sequence». Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. 47. σελίδες 45–148. doi:10.1002/9780470122921.ch2. ISBN 9780470122921. PMID 364941.

curtin.edu.au

biomed.curtin.edu.au

Steven Bottomley (2004). «Interactive Protein Structure Tutorial». Αρχειοθετήθηκε από το πρωτότυπο στις 1 Μαρτίου 2011. Ανακτήθηκε στις 9 Ιανουαρίου 2011.

doi.org

dx.doi.org

«Kaj Ulrik Linderstrøm-Lang (1896–1959)». Protein Sci. 6 (5): 1092–100. 1997. doi:10.1002/pro.5560060516. PMID 9144781. «He had already introduced the concepts of the primary, secondary, and tertiary structure of proteins in the third Lane Lecture (Linderstram-Lang, 1952)».
«Secondary structure and rigidity in model proteins». Soft Matter 9 (40): 9548–56. October 2013. doi:10.1039/C3SM50807B. PMID 26029761.
«Rigidity, secondary structure, and the universality of the boson peak in proteins». Biophysical Journal 106 (12): 2667–74. June 2014. doi:10.1016/j.bpj.2014.05.009. PMID 24940784.
«Coherent neutron scattering and collective dynamics in the protein, GFP». Biophys. J. 105 (9): 2182–87. 2013. doi:10.1016/j.bpj.2013.09.029. PMID 24209864.
«Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features». Biopolymers 22 (12): 2577–637. Dec 1983. doi:10.1002/bip.360221211. PMID 6667333. https://archive.org/details/sim_biopolymers_1983-12_22_12/page/2577.
«Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure». Proteins 3 (2): 71–84. 1988. doi:10.1002/prot.340030202. PMID 3399495.
«Knowledge-based protein secondary structure assignment». Proteins 23 (4): 566–79. Dec 1995. doi:10.1002/prot.340230412. PMID 8749853. Αρχειοθετήθηκε από το πρωτότυπο στις 2010-06-13. https://web.archive.org/web/20100613184204/http://nook.cs.ucdavis.edu/~koehl/Classes/ECS289/reprints/Paper_Stride.pdf. Ανακτήθηκε στις 2021-06-30.
«ScrewFit: combining localization and description of protein secondary structure». Acta Crystallographica Section D 68 (Pt 12): 1690–3. December 2012. doi:10.1107/s0907444912039029. PMID 23151634.
«Minimum message length inference of secondary structure from protein coordinate data». Bioinformatics 28 (12): i97–i105. Jun 2012. doi:10.1093/bioinformatics/bts223. PMID 22689785.
«Spectroscopic methods for analysis of protein secondary structure». Anal. Biochem. 277 (2): 167–76. 2000. doi:10.1006/abio.1999.4320. PMID 10625503.
«Rapid protein fold determination using unassigned NMR data». Proc. Natl. Acad. Sci. U.S.A. 100 (26): 15404–09. 2003. doi:10.1073/pnas.2434121100. PMID 14668443.
«Prediction of protein conformation». Biochemistry 13 (2): 222–45. Jan 1974. doi:10.1021/bi00699a002. PMID 4358940.
«Empirical predictions of protein conformation». Annual Review of Biochemistry 47: 251–76. 1978. doi:10.1146/annurev.bi.47.070178.001343. PMID 354496. https://archive.org/details/sim_annual-review-of-biochemistry_1978_47/page/251.
«Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins». Journal of Molecular Biology 120 (1): 97–120. March 1978. doi:10.1016/0022-2836(78)90297-8. PMID 642007.
«How good are predictions of protein secondary structure?». FEBS Letters 155 (2): 179–82. May 1983. doi:10.1016/0014-5793(82)80597-8. PMID 6852232.
«Integrating protein secondary structure prediction and multiple sequence alignment». Current Protein & Peptide Science 5 (4): 249–66. Aug 2004. doi:10.2174/1389203043379675. PMID 15320732.
«SAM-T08, HMM-based protein structure prediction». Nucleic Acids Res. 37 (Web Server issue): W492–97. 2009. doi:10.1093/nar/gkp403. PMID 19483096.
«Porter: a new, accurate server for protein secondary structure prediction». Bioinformatics 21 (8): 1719–20. 2005. doi:10.1093/bioinformatics/bti203. PMID 15585524.
«PredictProtein—an open resource for online prediction of protein structural and functional features». Nucleic Acids Res. 42 (Web Server issue): W337–43. 2014. doi:10.1093/nar/gku366. PMID 24799431.
«Combining prediction of secondary structure and solvent accessibility in proteins». Proteins 59 (3): 467–75. 2005. doi:10.1002/prot.20441. PMID 15768403.
«The effect of long-range interactions on the secondary structure formation of proteins». Protein Science 14 (8): 1955–963. Aug 2005. doi:10.1110/ps.051479505. PMID 15987894.
«Structural classification of thioredoxin-like fold proteins». Proteins 58 (2): 376–88. 2005. doi:10.1002/prot.20329. PMID 15558583. http://prodata.swmed.edu/Lab/Thiored_Proteins04.pdf. «Since the fold definition should include only the core secondary structural elements that are present in the majority of homologs, we define the thioredoxin-like fold as a two-layer α/β sandwich with the βαβββα secondary-structure pattern.».
«Alpha helices are more robust to mutations than beta strands». PLoS Computational Biology 12 (12): e1005242. 2016. doi:10.1371/journal.pcbi.1005242. PMID 27935949.
«Global analysis of protein folding using massively parallel design, synthesis, and testing». Science 357 (6347): 168–175. 2017. doi:10.1126/science.aan0693. PMID 28706065.

doi.org

Chou PY, Fasman GD (1978). «Prediction of the secondary structure of proteins from their amino acid sequence». Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. 47. σελίδες 45–148. doi:10.1002/9780470122921.ch2. ISBN 9780470122921. PMID 364941.
Pirovano W, Heringa J (2010). Protein secondary structure prediction. Methods Mol. Biol. Methods in Molecular Biology. 609. σελίδες 327–48. doi:10.1007/978-1-60327-241-4_19. ISBN 978-1-60327-240-7. PMID 20221928.

monash.edu.au

lcb.infotech.monash.edu.au

«SST web server». Ανακτήθηκε στις 17 Απριλίου 2018.

nih.gov

ncbi.nlm.nih.gov

«Kaj Ulrik Linderstrøm-Lang (1896–1959)». Protein Sci. 6 (5): 1092–100. 1997. doi:10.1002/pro.5560060516. PMID 9144781. «He had already introduced the concepts of the primary, secondary, and tertiary structure of proteins in the third Lane Lecture (Linderstram-Lang, 1952)».
«Secondary structure and rigidity in model proteins». Soft Matter 9 (40): 9548–56. October 2013. doi:10.1039/C3SM50807B. PMID 26029761.
«Rigidity, secondary structure, and the universality of the boson peak in proteins». Biophysical Journal 106 (12): 2667–74. June 2014. doi:10.1016/j.bpj.2014.05.009. PMID 24940784.
«Coherent neutron scattering and collective dynamics in the protein, GFP». Biophys. J. 105 (9): 2182–87. 2013. doi:10.1016/j.bpj.2013.09.029. PMID 24209864.
«Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features». Biopolymers 22 (12): 2577–637. Dec 1983. doi:10.1002/bip.360221211. PMID 6667333. https://archive.org/details/sim_biopolymers_1983-12_22_12/page/2577.
«Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure». Proteins 3 (2): 71–84. 1988. doi:10.1002/prot.340030202. PMID 3399495.
«Knowledge-based protein secondary structure assignment». Proteins 23 (4): 566–79. Dec 1995. doi:10.1002/prot.340230412. PMID 8749853. Αρχειοθετήθηκε από το πρωτότυπο στις 2010-06-13. https://web.archive.org/web/20100613184204/http://nook.cs.ucdavis.edu/~koehl/Classes/ECS289/reprints/Paper_Stride.pdf. Ανακτήθηκε στις 2021-06-30.
«ScrewFit: combining localization and description of protein secondary structure». Acta Crystallographica Section D 68 (Pt 12): 1690–3. December 2012. doi:10.1107/s0907444912039029. PMID 23151634.
«Minimum message length inference of secondary structure from protein coordinate data». Bioinformatics 28 (12): i97–i105. Jun 2012. doi:10.1093/bioinformatics/bts223. PMID 22689785.
«Spectroscopic methods for analysis of protein secondary structure». Anal. Biochem. 277 (2): 167–76. 2000. doi:10.1006/abio.1999.4320. PMID 10625503.
«Rapid protein fold determination using unassigned NMR data». Proc. Natl. Acad. Sci. U.S.A. 100 (26): 15404–09. 2003. doi:10.1073/pnas.2434121100. PMID 14668443.
«Prediction of protein conformation». Biochemistry 13 (2): 222–45. Jan 1974. doi:10.1021/bi00699a002. PMID 4358940.
«Empirical predictions of protein conformation». Annual Review of Biochemistry 47: 251–76. 1978. doi:10.1146/annurev.bi.47.070178.001343. PMID 354496. https://archive.org/details/sim_annual-review-of-biochemistry_1978_47/page/251.
Chou PY, Fasman GD (1978). «Prediction of the secondary structure of proteins from their amino acid sequence». Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. 47. σελίδες 45–148. doi:10.1002/9780470122921.ch2. ISBN 9780470122921. PMID 364941.
«Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins». Journal of Molecular Biology 120 (1): 97–120. March 1978. doi:10.1016/0022-2836(78)90297-8. PMID 642007.
«How good are predictions of protein secondary structure?». FEBS Letters 155 (2): 179–82. May 1983. doi:10.1016/0014-5793(82)80597-8. PMID 6852232.
«Integrating protein secondary structure prediction and multiple sequence alignment». Current Protein & Peptide Science 5 (4): 249–66. Aug 2004. doi:10.2174/1389203043379675. PMID 15320732.
Pirovano W, Heringa J (2010). Protein secondary structure prediction. Methods Mol. Biol. Methods in Molecular Biology. 609. σελίδες 327–48. doi:10.1007/978-1-60327-241-4_19. ISBN 978-1-60327-240-7. PMID 20221928.
«SAM-T08, HMM-based protein structure prediction». Nucleic Acids Res. 37 (Web Server issue): W492–97. 2009. doi:10.1093/nar/gkp403. PMID 19483096.
«Porter: a new, accurate server for protein secondary structure prediction». Bioinformatics 21 (8): 1719–20. 2005. doi:10.1093/bioinformatics/bti203. PMID 15585524.
«PredictProtein—an open resource for online prediction of protein structural and functional features». Nucleic Acids Res. 42 (Web Server issue): W337–43. 2014. doi:10.1093/nar/gku366. PMID 24799431.
«Combining prediction of secondary structure and solvent accessibility in proteins». Proteins 59 (3): 467–75. 2005. doi:10.1002/prot.20441. PMID 15768403.
«The effect of long-range interactions on the secondary structure formation of proteins». Protein Science 14 (8): 1955–963. Aug 2005. doi:10.1110/ps.051479505. PMID 15987894.
«Structural classification of thioredoxin-like fold proteins». Proteins 58 (2): 376–88. 2005. doi:10.1002/prot.20329. PMID 15558583. http://prodata.swmed.edu/Lab/Thiored_Proteins04.pdf. «Since the fold definition should include only the core secondary structural elements that are present in the majority of homologs, we define the thioredoxin-like fold as a two-layer α/β sandwich with the βαβββα secondary-structure pattern.».
«Alpha helices are more robust to mutations than beta strands». PLoS Computational Biology 12 (12): e1005242. 2016. doi:10.1371/journal.pcbi.1005242. PMID 27935949.
«Global analysis of protein folding using massively parallel design, synthesis, and testing». Science 357 (6347): 168–175. 2017. doi:10.1126/science.aan0693. PMID 28706065.

pubmedcentral.nih.gov

«Kaj Ulrik Linderstrøm-Lang (1896–1959)». Protein Sci. 6 (5): 1092–100. 1997. doi:10.1002/pro.5560060516. PMID 9144781. «He had already introduced the concepts of the primary, secondary, and tertiary structure of proteins in the third Lane Lecture (Linderstram-Lang, 1952)».
«Rigidity, secondary structure, and the universality of the boson peak in proteins». Biophysical Journal 106 (12): 2667–74. June 2014. doi:10.1016/j.bpj.2014.05.009. PMID 24940784.
«Coherent neutron scattering and collective dynamics in the protein, GFP». Biophys. J. 105 (9): 2182–87. 2013. doi:10.1016/j.bpj.2013.09.029. PMID 24209864.
«Minimum message length inference of secondary structure from protein coordinate data». Bioinformatics 28 (12): i97–i105. Jun 2012. doi:10.1093/bioinformatics/bts223. PMID 22689785.
«Rapid protein fold determination using unassigned NMR data». Proc. Natl. Acad. Sci. U.S.A. 100 (26): 15404–09. 2003. doi:10.1073/pnas.2434121100. PMID 14668443.
«SAM-T08, HMM-based protein structure prediction». Nucleic Acids Res. 37 (Web Server issue): W492–97. 2009. doi:10.1093/nar/gkp403. PMID 19483096.
«PredictProtein—an open resource for online prediction of protein structural and functional features». Nucleic Acids Res. 42 (Web Server issue): W337–43. 2014. doi:10.1093/nar/gku366. PMID 24799431.
«The effect of long-range interactions on the secondary structure formation of proteins». Protein Science 14 (8): 1955–963. Aug 2005. doi:10.1110/ps.051479505. PMID 15987894.
«Alpha helices are more robust to mutations than beta strands». PLoS Computational Biology 12 (12): e1005242. 2016. doi:10.1371/journal.pcbi.1005242. PMID 27935949.
«Global analysis of protein folding using massively parallel design, synthesis, and testing». Science 357 (6347): 168–175. 2017. doi:10.1126/science.aan0693. PMID 28706065.

swmed.edu

prodata.swmed.edu

«Structural classification of thioredoxin-like fold proteins». Proteins 58 (2): 376–88. 2005. doi:10.1002/prot.20329. PMID 15558583. http://prodata.swmed.edu/Lab/Thiored_Proteins04.pdf. «Since the fold definition should include only the core secondary structural elements that are present in the majority of homologs, we define the thioredoxin-like fold as a two-layer α/β sandwich with the βαβββα secondary-structure pattern.».

ucdavis.edu

nook.cs.ucdavis.edu

«Knowledge-based protein secondary structure assignment». Proteins 23 (4): 566–79. Dec 1995. doi:10.1002/prot.340230412. PMID 8749853. Αρχειοθετήθηκε από το πρωτότυπο στις 2010-06-13. https://web.archive.org/web/20100613184204/http://nook.cs.ucdavis.edu/~koehl/Classes/ECS289/reprints/Paper_Stride.pdf. Ανακτήθηκε στις 2021-06-30.

web.archive.org

Steven Bottomley (2004). «Interactive Protein Structure Tutorial». Αρχειοθετήθηκε από το πρωτότυπο στις 1 Μαρτίου 2011. Ανακτήθηκε στις 9 Ιανουαρίου 2011.
«Knowledge-based protein secondary structure assignment». Proteins 23 (4): 566–79. Dec 1995. doi:10.1002/prot.340230412. PMID 8749853. Αρχειοθετήθηκε από το πρωτότυπο στις 2010-06-13. https://web.archive.org/web/20100613184204/http://nook.cs.ucdavis.edu/~koehl/Classes/ECS289/reprints/Paper_Stride.pdf. Ανακτήθηκε στις 2021-06-30.

worldcat.org

Schulz, G. E. (1979). Principles of protein structure. Schirmer, R. Heiner, 1942-. New York: Springer-Verlag. ISBN 0-387-90386-0. OCLC 4498269.