The Ising model for prediction of disordered residues from protein sequence alone

被引:57
作者
Lobanov, Michail Yu [1 ]
Galzitskaya, Oxana V. [1 ]
机构
[1] Russian Acad Sci, Inst Prot Res, Pushchino 142290, Moscow Region, Russia
来源
PHYSICAL BIOLOGY | 2011年 / 8卷 / 03期
基金
俄罗斯基础研究基金会;
关键词
INTRINSICALLY UNSTRUCTURED PROTEINS; AMINO-ACID-COMPOSITION; ENERGY CONTENT; WEB SERVER; REGIONS; CHAIN;
D O I
10.1088/1478-3975/8/3/035004
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Intrinsically disordered regions serve as molecular recognition elements, which play an important role in the control of many cellular processes and signaling pathways. It is useful to be able to predict positions of disordered residues and disordered regions in protein chains using protein sequence alone. A new method (IsUnstruct) based on the Ising model for prediction of disordered residues from protein sequence alone has been developed. According to this model, each residue can be in one of two states: ordered or disordered. The model is an approximation of the Ising model in which the interaction term between neighbors has been replaced by a penalty for changing between states (the energy of border). The IsUnstruct has been compared with other available methods and found to perform well. The method correctly finds 77% of disordered residues as well as 87% of ordered residues in the CASP8 database, and 72% of disordered residues as well as 85% of ordered residues in the DisProt database.
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页数:9
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