Effective potentials for folding proteins

被引：24

作者：

Chen, NY ^{[1
]}

Su, ZY

Mou, CY

机构：

[1] Acad Sinica, Inst Phys, Taipei 11529, Taiwan

[2] Natl Tsing Hua Univ, Dept Phys, Hsinchu, Taiwan

[3] Natl Ctr High Performance Comp, Hsinchu, Taiwan

[4] Natl Ctr Theoret Sci, Div Phys, Hsinchu, Taiwan

来源：

PHYSICAL REVIEW LETTERS | 2006年 / 96卷 / 07期

关键词：

D O I：

10.1103/PhysRevLett.96.078103

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

A coarse-grained off-lattice model that is not biased in any way to the native state is proposed to fold proteins. To predict the native structure in a reasonable time, the model has included the essential effects of water in an effective potential. Two new ingredients, the dipole-dipole interaction and the local hydrophobic interaction, are introduced and are shown to be as crucial as the hydrogen bonding. The model allows successful folding of the wild-type sequence of protein G and may have provided important hints to the study of protein folding.

引用

页数：4

共 24 条

[1] SPECIFIC NUCLEUS AS THE TRANSITION-STATE FOR PROTEIN-FOLDING - EVIDENCE FROM THE LATTICE MODEL [J].