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Protein Engineering, Vol. 13, No. 6, 407-412, June 2000
© 2000 Oxford University Press

ß-Sheet modeling by helical surfaces

Denis Znamenskiy, Khan Le Tuan, Anne Poupon, Jacques Chomilier1 and Jean-Paul Mornon

Equipe Systèmes Moléculaires et Biologie Structurale, LMCP, CNRS UMR7590, Universités Paris 6 et Paris 7, Case 115, 75252 Paris cedex 05, France

We present a topological description of a ß-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 ß-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 ß-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.


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D. Znamenskiy, J. Chomilier, K. Le Tuan, and J.-P. Mornon
A new protein folding algorithm based on hydrophobic compactness: Rigid Unconnected Secondary Structure Iterative Assembly (RUSSIA). I: Methodology
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