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Comparison of Super-secondary Structures in Proteins

Journal of Molecular Biology, 1973
Abstract A method of comparing the conformations of different, but structurally related proteins is described. Local variations, such as the systematic translation of a helix, or the position of deletions and insertions can be detected, and the correspondence of only marginally similar structures can be measured.
S T, Rao, M G, Rossmann
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Modeling secondary structures and secondary structure linkages of protein sequences

2010 IEEE International Conference on Systems, Man and Cybernetics, 2010
In this paper we model protein secondary structures such as a-helices and b sheets and linkages thereof using passive electrical circuit components and obtain the frequency responses of these circuits. An analysis of the frequency responses of these model circuits shows that putative connections can be made between circuit behavior and known ...
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Protein Secondary Structure Prediction

2009
While the prediction of a native protein structure from sequence continues to remain a challenging problem, over the past decades computational methods have become quite successful in exploiting the mechanisms behind secondary structure formation. The great effort expended in this area has resulted in the development of a vast number of secondary ...
Pirovano, W.A., Heringa, J.
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On the pathway of the formation of secondary structures in proteins

Proteins: Structure, Function, and Bioinformatics, 2023
AbstractProtein structures are typically made up of well‐defined modules, called secondary structures. A hierarchical model of protein folding may start with the formation of five‐membered non‐covalently‐linked ring motifs involving O⋅⋅⋅C=O and N−H···N interactions connecting two consecutive peptide groups.
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The role of secondary structure in protein structure selection

The European Physical Journal E, 2010
The presence of highly regular secondary structure motifs in protein structure is a fascinating area of study. The secondary structures play important roles in protein structure and protein folding. We investigate the folding properties of protein by introducing the effect of secondary structure elements. We observed the emergence of several structures
Yong-Yun, Ji, You-Quan, Li
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Uncertainty Visualization for Secondary Structures of Proteins

2018 IEEE Pacific Visualization Symposium (PacificVis), 2018
We present a technique that conveys the uncertainty in the secondary structure of proteins—an abstraction model based on atomic coordinates. While protein data inherently contains uncertainty due to the acquisition method or the simulation algorithm, we argue that it is also worth investigating uncertainty induced by analysis algorithms that precede ...
Christoph Schulz 0001   +5 more
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Evaluation of secondary structure predictions in proteins

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1977
Data of 33 proteins are used to compare four methods which predict secondary structure from the amino acid sequence. The prediction of alpha-helices according to the histogram method of Argos et al. (Argos, P., Schwarz, J. and Schwarz, J. (1976) Biochim. Biophys.
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The protein secondary structure flexibility

2008
Modeling protein flexibility is a long standing challenge in computational biology with a special impact to protein docking. Relating problems are protein structures alignment and identification of flexible and rigid protein regions, as well as a general definition of a region degree of flexibility.
Šikić, Krešimir   +2 more
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Protein secondary structure

International Journal of Peptide and Protein Research, 1982
A secondary structure prediction technique is proposed which includes nucleation site determination through multiplication of conformational preference parameters as well as weighting factors to represent structurally stabilizing short range interactions.
J, Palau, P, Argos, P, Puigdomenech
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Evaluating Predictions of Secondary Structure in Proteins

Biochemical and Biophysical Research Communications, 1994
To learn how secondary structure assignments diverge during divergent evolution, pairs of proteins with solved crystal structures were aligned and their assignments compared as a function of evolutionary distance. Residues assigned in one structure to a helix or a strand are frequently paired with residues assigned in the other to a coil.
T F, Jenny, S A, Benner
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