Results 11 to 20 of about 977,591 (119)
Linkers of secondary structures in proteins [PDF]
Protein Science, 1997 AbstractLinkers that connect repeating secondary structures fall into conformational classes based on distance and main‐chain torsion clustering. A data set of 300 unique protein chains with low pairwise sequence identity was clustered into only a few groups representing the preferred motifs.
V, Geetha, P J, Munson
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Comparative visualization of protein secondary structures [PDF]
BMC Bioinformatics, 2017 Protein function is determined by many factors, namely by its constitution, spatial arrangement, and dynamic behavior. Studying these factors helps the biochemists and biologists to better understand the protein behavior and to design proteins with modified properties.
Lucia Kocincová +5 more
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Bayesian Segmentation of Protein Secondary Structure [PDF]
Journal of Computational Biology, 2000 We present a novel method for predicting the secondary structure of a protein from its amino acid sequence. Most existing methods predict each position in turn based on a local window of residues, sliding this window along the length of the sequence. In contrast, we develop a probabilistic model of protein sequence/structure relationships in terms of ...
Scott C. Schmidler +2 more
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Properties and origins of protein secondary structure [PDF]
Physical Review E, 1994 12 pages (+4 figures, included in a single postscript file), LaTeX + RevTeX 3 ...
Socci, Nicholas D. +2 more
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SSEP: secondary structural elements of proteins [PDF]
Nucleic Acids Research, 2003 SSEP is a comprehensive resource for accessing information related to the secondary structural elements present in the 25 and 90% non-redundant protein chains. The database contains 1771 protein chains from 1670 protein structures and 6182 protein chains from 5425 protein structures in 25 and 90% non-redundant protein chains, respectively.
Shanthi, V +4 more
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The hydration of protein secondary structures
FEBS Letters, 1987 The hydration of the main‐chain carbonyl (CO) groups in proteins have been studied using infra‐red spectroscopy, and computer‐graphics analysis of high resolution protein crystal structures. The IR measurements indicate that the strength of water binding to the CO groups is lower in β‐sheet proteins compared with α‐helical ones. Analysis of the protein
Barlow, D.J., Poole, P.L.
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Extended secondary structures in proteins
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2014 Super secondary structures of proteins have been systematically searched and classified, but not enough attention has been devoted to such large edifices beyond the basic identification of secondary structures. The objective of the present study is to show that the association of secondary structures that share some of their backbone residues is a ...
Degrève, Léo +2 more
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Prediction of protein secondary structure content [PDF]
Protein Engineering, Design and Selection, 1999 All existing algorithms for predicting the content of protein secondary structure elements have been based on the conventional amino-acid-composition, where no sequence coupling effects are taken into account. In this article, an algorithm was developed for predicting the content of protein secondary structure elements that was based on a new amino ...
W, Liu, K C, Chou
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Secondary structure determines protein topology [PDF]
Protein Science, 2006 AbstractUsing a test set of 13 small, compact proteins, we demonstrate that a remarkably simple protocol can capture native topology from secondary structure information alone, in the absence of long‐range interactions. It has been a long‐standing open question whether such information is sufficient to determine a protein's fold.
Patrick J, Fleming +2 more
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A physical basis for protein secondary structure [PDF]
Proceedings of the National Academy of Sciences, 1999 A physical theory of protein secondary structure is proposed and tested by performing exceedingly simple Monte Carlo simulations. In essence, secondary structure propensities are predominantly a consequence of two competing local effects, one favoring hydrogen bond formation in helices and turns, the other opposing the attendant reduction in sidechain ...
R, Srinivasan, G D, Rose
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