Voronoi tessellation reveals the condensed matter character of folded proteins

被引：55

作者：

Soyer, A

Chomilier, J

Mornon, JP

Jullien, R

Sadoc, JF

机构：

[1] Univ Paris 06, CNRS, Lab Mineral Cristallog, F-75252 Paris, France

[2] Univ Paris 07, CNRS, Lab Mineral Cristallog, F-75252 Paris, France

[3] Univ Montpellier 2, CNRS, Lab Verres, F-34095 Montpellier, France

[4] Univ Paris 11, Ctr Orsay, CNRS, Phys Solides Lab, F-91405 Orsay, France

来源：

PHYSICAL REVIEW LETTERS | 2000年 / 85卷 / 16期

关键词：

D O I：

10.1103/PhysRevLett.85.3532

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

The packing geometry of amino acids in folded proteins is analyzed via a modified Voronoi tessellation method which distinguishes bulk and surface. From a statistical analysis of the Voronoi cells over 40 representative proteins, it appears that the packings are in average similar to random packings of hard spheres encountered in condensed matter physics, with a quite strong fivefold local symmetry. Moreover, the statistics permits one to establish a classification of amino acids in terms of increasing propensity to be buried in agreement with what is known from chemical considerations.

引用

页码：3532 / 3535

页数：4

共 31 条

[1] CONSERVATION OF POLYPROLINE-II HELICES IN HOMOLOGOUS PROTEINS - IMPLICATIONS FOR STRUCTURE PREDICTION BY MODEL-BUILDING [J].