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Abstract:
An effective and fast minimization approach is proposed for the prediction of protein folding, in which the 'relative entropy' is used as a minimization function and the off- lattice model is used. In this approach, we only use the information of distances between the consecutive C-alpha atoms along the peptide chain and a generalized form of the contact potential for 20 types of amino acids. Tests of the algorithm are performed on the real proteins. The root mean square deviations of the structures of eight folded target proteins versus the native structures are in a reasonable range. In principle, this method is an improvement on the energy minimization approach.
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PROTEIN ENGINEERING
ISSN: 0269-2139
Year: 2003
Issue: 9
Volume: 16
Page: 659-663
JCR Journal Grade:2
Cited Count:
WoS CC Cited Count: 9
SCOPUS Cited Count: 8
ESI Highly Cited Papers on the List: 0 Unfold All
WanFang Cited Count:
Chinese Cited Count:
30 Days PV: 1
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