多链蛋白质的从头折叠
Ab initio folding of multiple-chain proteins.
作者信息
Saunders J A, Gibson K D, Scheraga H A
机构信息
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA.
出版信息
Pac Symp Biocomput. 2002:601-12. doi: 10.1142/9789812799623_0056.
PMID:11928512
Abstract
Our previous methodology for ab initio prediction of protein structure is extended here to treat multiple-chain proteins. This involved modification of our united-residue (UNRES) force field and our Conformational Space Annealing (CSA) Global Optimization procedure. Good results have been obtained for both a four- and a three-helix protein from the CASP3 exercise.
摘要
我们先前用于从头预测蛋白质结构的方法在此得到扩展，以处理多链蛋白质。这涉及对我们的联合残基（UNRES）力场和构象空间退火（CSA）全局优化程序进行修改。对于来自CASP3实验的一种四螺旋蛋白质和一种三螺旋蛋白质，均已获得了良好的结果。
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