Results 1 to 10 of about 827,340 (267)
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.
P. J. Munson, V. Geetha
openaire +3 more sources
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.
Helwig Hauser +6 more
openaire +5 more sources
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 ...
Nicholas D. Socci +5 more
openaire +3 more sources
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 ...
Léo Degrève +2 more
openaire +3 more sources
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
P.L. Poole, David J. Barlow
openaire +3 more sources
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
openaire +3 more sources
A Kernel for Protein Secondary Structure Prediction [PDF]
, 2004 Multi-class support vector machines have already proved efficient in protein secondary structure prediction as ensemble methods, to combine the outputs of sets of classifiers based on different principles. In this chapter, their implementation as basic prediction methods, processing the primary structure or the profile of multiple alignments, is ...
Guermeur, Yann +2 more
openaire +3 more sources
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 ...
Douglas L. Brutlag +2 more
openaire +3 more sources
Electrostatic interactions and secondary structures in proteins
Biophysical Journal, 1980 In an attempt to understand the occurrences of secondary forms in proteins, we have calculated approximate free energies for a large set of regular secondary regions and have compared several methods for choosing a single molecular conformation. Approximate conformational free energies have been obtained by directly calculating electrostatic energies ...
Shousun C. Szu +2 more
openaire +3 more sources
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.
George D. Rose +2 more
openaire +3 more sources