The contribution of metal ions to the conformational stability of ribonuclease T1 -: Crystal versus solution

被引：17

作者：

Deswarte, J ^{[1
]}

De Vos, S ^{[1
]}

Langhorst, U ^{[1
]}

Steyaert, J ^{[1
]}

Loris, R ^{[1
]}

机构：

[1] Free Univ Brussels VIB, Lab Ultrastruct, B-1640 Rhode St Genese, Belgium

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 2001年 / 268卷 / 14期

关键词：

conformational stability; metal binding; RNase T-1;

D O I：

10.1046/j.1432-1327.2001.02310.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：

In the crystalline state, ribonuclease T-1 binds calcium ions at different lattice-dependent positions. In solution, its conformational stability is also remarkably increased in the presence of divalent metal ions. Combining urea unfolding studies and X-ray crystallography, we compared the presence of several metal ions at specific sites in the protein to their contribution to the overall stabilizing effect in solution. We constructed thermodynamic cycles involving particular metal ions and specific carboxylate functions. The resulting coupling energies indicate that some (but not all) metal ions found at lattice contacts in crystal structures may indeed significantly contribute to stability enhancement in the presence of metal ions in solution.

引用

页码：3993 / 4000

页数：8

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