CAN THE STRUCTURE OF PROTEINS BE CALCULATED

被引：6

作者：

JAHNIG, F ^{[1
]}

EDHOLM, O ^{[1
]}

机构：

[1] ROYAL INST TECHNOL, DEPT THEORET PHYS, S-10044 STOCKHOLM 70, SWEDEN

来源：

ZEITSCHRIFT FUR PHYSIK B-CONDENSED MATTER | 1990年 / 78卷 / 01期

关键词：

D O I：

10.1007/BF01317366

中图分类号：

O469 [凝聚态物理学];

学科分类号：

070205 ;

摘要：

In contrast to soluble proteins, membrane proteins offer the possibility, to predict their secondary structure with some reliability. Based on such predictions a set of initial conformation can be constructed on which molecular dynamics simulations are performed in order to find the most stable state. The important point is that all those degrees of freedom which change slowly in time must be varied artificially in the set of initial conformations. This procedure is demonstrated for the membrane protein bacteriorhodopsin. © 1990 Springer-Verlag.

引用

页码：137 / 143

页数：7

共 23 条

[21] 3-DIMENSIONAL STRUCTURE OF DEOXYCHOLATE-TREATED PURPLE MEMBRANE AT 6 A RESOLUTION AND MOLECULAR AVERAGING OF 3 CRYSTAL FORMS OF BACTERIORHODOPSIN
TSYGANNIK, IN
BALDWIN, JM
[J]. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 1987, 14 (05): : 263 - 272
[22] EFFECT OF CONSTRAINTS ON THE DYNAMICS OF MACROMOLECULES
VANGUNSTEREN, WF
KARPLUS, M
[J]. MACROMOLECULES, 1982, 15 (06) : 1528 - 1544
[23] LOCATION OF THE CARBOXYL TERMINUS OF BACTERIORHODOPSIN IN PURPLE MEMBRANE
WALLACE, BA
HENDERSON, R
[J]. BIOPHYSICAL JOURNAL, 1982, 39 (03) : 233 - 239

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