A theoretical method is proposed to identify structural domains in proteins of known structures. It is based on the distribution of the local axes of the polypeptide chain. In particular, a statistical analysis is applied to the contributions of the local axes to the absolute writhing number, a topological property of a space curve resulting from the number of self-crossings in the curve projections onto a unit sphere. This finding supports the hypothesis that topological requirements should be satisfied in the process of protein folding and in the final organization of the tertiary structures. (C) 2001 John Wiley & Sons, Inc. Biopoly 58. 218-229, 2001.
Anselmi, C., Bocchinfuso, G., Scipioni, A., De Santis, P. (2001). Identification of protein domains on topological basis. BIOPOLYMERS, 58(2), 218-229 [10.1002/1097-0282(200102)58:2<218::AID-BIP100>3.0.CO;2-M].
Identification of protein domains on topological basis
Bocchinfuso, G.;
2001-01-01
Abstract
A theoretical method is proposed to identify structural domains in proteins of known structures. It is based on the distribution of the local axes of the polypeptide chain. In particular, a statistical analysis is applied to the contributions of the local axes to the absolute writhing number, a topological property of a space curve resulting from the number of self-crossings in the curve projections onto a unit sphere. This finding supports the hypothesis that topological requirements should be satisfied in the process of protein folding and in the final organization of the tertiary structures. (C) 2001 John Wiley & Sons, Inc. Biopoly 58. 218-229, 2001.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
