Ab initio protein folding

被引:83
作者
Osguthorpe, DJ [1 ]
机构
[1] Univ Bath, Dept Chem, Bath BA2 7AY, Avon, England
关键词
D O I
10.1016/S0959-440X(00)00067-1
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
Ab initio protein folding methods have been developing rapidly over the past few years and, at the last Critical assessment of methods of protein structure prediction (CASP) meeting, it was shown that important progress has been made in generating structure from sequence. Both methods based on statistical potentials and methods using physics-based potentials have shown improvements. Most current methods use statistics-based potentials and the development of these is ongoing. Additionally, the inclusion of multiple sequence data in the algorithms in order to aid in finding the native structure is a common theme. The use of physics-based potentials is less developed, which means that less progress has been made in understanding why a sequence forms a structure.
引用
收藏
页码:146 / 152
页数:7
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