beta sheet

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beta sheet

n.
A secondary structure that occurs in many proteins and consists of two or more parallel adjacent polypeptide chains arranged in such a way that hydrogen bonds can form between the chains. Also called beta pleated sheet, pleated sheet.

[From beta-form, the form taken by a protein molecule after it has been stretched.]
References in periodicals archive ?
This is indicative of an overall increase in beta-sheet content of the sample; we ascribe this increase in amplitude to growth of the beta-fibrils in the sample.
The repeated GAGAGS peptide sequences are frequently seen in the beta-sheet structure, forming crystallized regions in silk fiber and silk films [12].
"Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation".
Recently, scientists also discovered that the suckerin proteins are comprised of "beta-sheet" polymer networks that are thermoplastic (meaning that they melt when heated and harden when cooled).
He, "Beta-sheet detection and representation from medium resolution cryo-EM density maps," in Proceedings of the 4th ACM Conference on Bioinformatics, Computational Biology and Biomedical Informatics (BCB '13), pp.
The amino acid sequence stretches in the [XynA.sub.MG1] molecule predicted to form different secondary structures (alphahelices, beta-sheet, and loops) are shown in Figure 3(a).
Li, "Inhibition of aggregation of amyloid peptides by beta-sheet breaker peptides and their binding affinity," The Journal of Physical Chemistry B, vol.
Alpha-helix rods and folded beta-sheet constructions were clearly visible within the 20 subunits of the APC/C, defining the overall architecture of the complex.
The study of the secondary structure using circular dichroism (CD) (Figure 3) revealed that the peptide PB1 (625) in solution has a structure similar to the described model of beta-hairpin obtained using molecular dynamics methods (8% of alpha-helix, 30% of antiparallel beta-sheet, 25% of beta-turns, and 37% of random coil structure).
3B and D) corresponds to beta-sheet. Therefore, in the wild type protein the isoleucine at 474th position (indicated by the red dot in Fig.
Brunak, "Matching protein beta-sheet partners by feedforward and recurrent neural networks." in Proceedings of International Conference on Intelligent Systems for Molecular Biology (ISMB '00), vol.
Pulling geometry defines the mechanical resistance of a beta-sheet protein, Nat Struct Biol 2003; 10 (9): 731-737.