Kinetic stabilisation of a modular protein by domain interactions

被引：25

作者：

Wenk, M ^{[1
]}

Jaenicke, R ^{[1
]}

Mayr, EM ^{[1
]}

机构：

[1] Univ Regensburg, Inst Biophys & Phys Biochem, D-93040 Regensburg, Germany

来源：

FEBS LETTERS | 1998年 / 438卷 / 1-2期

关键词：

beta gamma-crystallin; domain folding; differential scanning calorimetry; kinetic stabilization; two-domain protein; domain interaction;

D O I：

10.1016/S0014-5793(98)01287-3

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：

Protein S, a two-domain spore coat protein from Myxococcus xanthus, is structurally related to eye-lens beta gamma-crystallins. No natural monomeric one-domain member of this protein superfamily is known. To determine the stability of the single domains and to explain the ubiquitous domain duplication, the isolated domains of protein S were constructed. The N-domain is thermodynamically more stable than the C-domain, In intact protein S, domain interactions lead to an apparent decrease in stability of the N-terminal domain, whereas the C-terminal domain is stabilised, In contrast, unfolding kinetics of both domains are decreased 100-fold due to interactions in the complete molecule. (C) 1998 Federation of European Biochemical Societies.

引用

页码：127 / 130

页数：4

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