Stability study of Rhodobacter capsulatus ferrocytochrome c(2) wild-type and site-directed mutants using hydrogen deuterium exchange monitored by electrospray ionization mass spectrometry

被引：16

作者：

Jaquinod, M

Guy, P

Halgand, F

Caffrey, M

Fitch, J

Cusanovich, M

Forest, E

机构：

[1] CNRS,CEA,INST BIOL STRUCT JEAN PIERRE EBEL,F-38027 GRENOBLE 1,FRANCE

[2] UNIV ARIZONA,DEPT BIOCHEM,TUCSON,AZ 85721

来源：

FEBS LETTERS | 1996年 / 380卷 / 1-2期

关键词：

electrospray ionization mass spectrometry; hydrogen/deuterium exchange; conformational stability; Rhodobacter capsulatus cytochrome c(2);

D O I：

10.1016/0014-5793(96)00004-X

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：

To estimate the stability of Rhodobacter capsulatus ferrocytochrome c(2) wild-type and site-directed mutants, charge state distributions and hydrogen/deuterium exchange rates mere monitored by electrospray ionization mass spectrometry, The relative stability of the mutants was observed with the order: V11 insert > Y75F > wild-type = K32E > K12D = K14E greater than or equal to K52E > K14E/K32E > W67Y > P35A > I57N > G34S, (A preliminary account has been presented for mutants G34S and P35A [Jaquinod et al, (1995) Rapid Commun, Mass Spectrom, 9, 1135-1140].) This approach is shown to be a useful tool for rapid characterization of mutational effects on protein conformation.

引用

页码：44 / 48

页数：5

共 37 条

[1] MASS-SPECTROMETRIC CHARACTERIZATION OF A PROTEIN LIGAND INTERACTION [J].