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Structure of coiled beta-beta-hairpins and beta-beta-corners.

Authors: A V, Efimov;

Structure of coiled beta-beta-hairpins and beta-beta-corners.

Abstract

Two types of super-secondary structure, coiled beta-beta-hairpins and beta-beta-corners, are considered in this paper. A beta-beta-corner can be represented as a long beta-beta-hairpin folded orthogonally on itself so that the strands, when passing from one layer to the other, rotate in a right-handed direction about an imaginary axis. It is shown that a beta-beta-hairpin, forming a coiled coil structure or a beta-beta-corner, is right-handed when viewed from the concave side. These unique arrangements of beta-strands in the coiled beta-beta-hairpins and beta-beta-corners are of particular value in protein modelling and prediction.

Related Organizations
Keywords

Ribonucleases, L-Lactate Dehydrogenase, Protein Conformation, Endopeptidases, Alcohol Dehydrogenase, Trypsin Inhibitors, Interleukin-1

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Powered by OpenAIRE graph
Found an issue? Give us feedback
selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
42
Average
Top 10%
Top 10%
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