Unfolded in vacuo lysozyme folds into native, quasinative, and compact structures

被引：42

作者：

Arteca, GA

Velázquez, I

Reimann, CT

Tapia, O

机构：

[1] Uppsala Univ, Dept Phys Chem, S-75121 Uppsala, Sweden

[2] Laurentian Univ, Dept Chim & Biochim, Sudbury, ON P3E 2C6, Canada

[3] Uppsala Univ, Dept Mat Sci, Div Ion Phys, S-75121 Uppsala, Sweden

来源：

PHYSICAL REVIEW E | 1999年 / 59卷 / 05期

关键词：

D O I：

10.1103/PhysRevE.59.5981

中图分类号：

O35 [流体力学]; O53 [等离子体物理学];

学科分类号：

070204 ; 080103 ; 080704 ;

摘要：

We show that the relaxation dynamics of unfolded in vacuo lysozyme is not random. Analyses of molecular dynamics trajectories in a convenient space of molecular shape descriptors reveal a "favored" pattern of transitions leading to stable conformations. The relaxation paths exhibit a balanced change in shape features: globular spheroids are formed slowly enough to allow the proper entanglement of secondary-structural elements. The present study shows that a protein in vacuo can actually (re)fold into native and quasinative structures. The driving force for these transformations is intrinsic to the polypeptide chain. [S1063-651X(99)12605-9].

引用

页码：5981 / 5986

页数：6

共 36 条

[1] A MOLECULAR-DYNAMICS STUDY OF THE C-TERMINAL FRAGMENT OF THE L7/L12 RIBOSOMAL-PROTEIN - SECONDARY STRUCTURE MOTION IN A 150 PICOSECOND TRAJECTORY [J].