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Protein Eng ; 13(6): 407-12, 2000 Jun.
Article in English | MEDLINE | ID: mdl-10877851

ABSTRACT

We present a topological description of a beta-sheet in terms of a piece of helical surface. It requires only two easy-to-handle parameters: the twist, i.e. the turn of the helical surface per residue, and the coiling, which is a curvature along the strands or in the direction perpendicular to the strands of the sheet. This method applies fairly well to three- and four-strand sheets, forming a too limited structure to be able to build a barrel. From an analysis of beta-sheets derived from a structural database, we show that this picture can even be reduced to the use of one main value, the twist angle. The dependence of beta-sheet twisting on the number of strands in a sheet, and also on the length and direction of strands, has been demonstrated. The applications of such a description may include the rapid modeling of 3D structures.


Subject(s)
Computer Simulation , Databases, Factual , Models, Chemical , Protein Structure, Secondary , Proteins/chemistry , Computational Biology/methods , Predictive Value of Tests , Proteins/classification
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