Folding, design, and determination of interaction potentials using off-lattice dynamics of model heteropolymers

被引：47

作者：

Clementi, C

Maritan, A

Banavar, JR

机构：

[1] SISSA, Int Sch Adv Studies, I-34014 Trieste, Italy

[2] Ist Nazl Fis Mat, I-34014 Trieste, Italy

[3] Abdus Salam Int Ctr Theoret Phys, I-34014 Trieste, Italy

[4] Penn State Univ, Dept Phys, Davey Lab 104, University Pk, PA 16802 USA

[5] Penn State Univ, Ctr Phys Mat, Davey Lab 104, University Pk, PA 16802 USA

来源：

PHYSICAL REVIEW LETTERS | 1998年 / 81卷 / 15期

关键词：

D O I：

10.1103/PhysRevLett.81.3287

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

We present the results of a self-consistent, unified molecular dynamics study of simple model heteropolymers in the continuum with emphasis on folding, sequence design, and the determination of the interaction parameters of the effective potential between the amino acids from the knowledge of the native states of the designed sequences. [S0031-9007(98)07313-X].

引用

页码：3287 / 3290

页数：4

共 22 条

[1]

[Anonymous], FOLDING DESIGN

[2] FUNNELS, PATHWAYS, AND THE ENERGY LANDSCAPE OF PROTEIN-FOLDING - A SYNTHESIS [J].