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Beta sheets consist of beta strands (β-strands) connected laterally by at least two or three backbone hydrogen bonds, forming a generally twisted, pleated sheet. A β-strand is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an extended conformation .
SST detects π and 3 10 helical caps to standard α-helices, and automatically assembles the various extended strands into consistent β-pleated sheets. It provides a readable output of dissected secondary structural elements, and a corresponding PyMol -loadable script to visualize the assigned secondary structural elements individually.
All beta-barrels can be classified in terms of two integer parameters: the number of strands in the beta-sheet, n, and the "shear number", S, a measure of the stagger of the strands in the beta-sheet. [3] These two parameters (n and S) are related to the inclination angle of the beta strands relative to the axis of the barrel. [4] [5] [6]
The immunoglobulin domain, also known as the immunoglobulin fold, is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology, [1] [2] consisting of about 125 amino acids. The backbone switches repeatedly between the two β-sheets.
The beta hairpin (sometimes also called beta-ribbon or beta-beta unit) is a simple protein structural motif involving two beta strands that look like a hairpin. The motif consists of two strands that are adjacent in primary structure , oriented in an antiparallel direction (the N-terminus of one sheet is adjacent to the C-terminus of the next ...
Beta barrels from eight beta-strands and with "shear number" of ten (n=8, S=10). They include: OmpA-like transmembrane domain (OmpA) Virulence-related outer membrane protein family (OmpX) Outer membrane protein W family (OmpW) Antimicrobial peptide resistance and lipid A acylation protein family (PagP) Lipid A deacylase PagL; Opacity family ...
Beta-sandwich or β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel beta sheets (β-sheets). [ 1 ] The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds.
Porins are composed of beta sheets (β sheets) made up of beta strands (β strands) which are linked together by beta turns (β turns) on the cytoplasmic side and long loops of amino acids on the other. The β strands lie in an antiparallel fashion and form a cylindrical tube, called a beta barrel (β barrel). [2]