Perspectives in protein-fold recognition

被引:51
|
作者
Torda, AE
机构
[1] Research School of Chemistry, Australian National University, Canberra
关键词
D O I
10.1016/S0959-440X(97)80026-7
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
Fold recognition force fields based on statistics from native structures have become commonplace. New, nonphysical force fields based on optimizing parameters rather than reflecting Boltzmann statistics may offer improvement in force-field performance for threading and other applications. Improvements in sequence-to-structure alignments will also be essential for improved fold recognition.
引用
收藏
页码:200 / 205
页数:6
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