CAN THE STABILITY OF PROTEIN MUTANTS BE PREDICTED BY FREE-ENERGY CALCULATIONS

被引：92

作者：

YUNYU, S

MARK, AE

WANG, CX

HUANG, FH

BERENDSEN, HJC

VANGUNSTEREN, WF

机构：

[1] SWISS FED INST TECHNOL,DEPT PHYS CHEM,CH-8092 ZURICH,SWITZERLAND

[2] UNIV SCI & TECHNOL CHINA,DEPT BIOL,HEFEI 230026,PEOPLES R CHINA

[3] UNIV GRONINGEN,PHYS CHEM LAB,9747 AG GRONINGEN,NETHERLANDS

来源：

PROTEIN ENGINEERING | 1993年 / 6卷 / 03期

关键词：

FREE ENERGY; MOLECULAR DYNAMICS; PROTEIN STABILITY; SUBTILISIN;

D O I：

10.1093/protein/6.3.289

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The use of free energy simulation techniques in the study of protein stability is critically evaluated. Results from two simulations of the thermostability mutation Asn218 to Ser218 in Subtilisin are presented. It is shown that components of the free energy change can be highly sensitive to the computational details of the simulation leading to the conclusion that free energy calculations cannot currently be used to reliably predict protein stability. The different factors that undermine the reliability are discussed.

引用

页码：289 / 295

页数：7

共 35 条

[1] REPLACEMENTS OF PRO86 IN PHAGE-T4 LYSOZYME EXTEND AN ALPHA-HELIX BUT DO NOT ALTER PROTEIN STABILITY [J].