The "Two-state folder" MerP forms partially unfolded structures that show temperature dependent hydrogen exchange

被引：7

作者：

Brorsson, AC

Kjellson, A

Aronsson, G

Sethson, I

Hambraeus, C

Jonsson, BH ^{[1
]}

机构：

[1] Linkoping Univ, IFM, SE-58183 Linkoping, Sweden

[2] Umea Univ, Dept Biochem, S-90187 Umea, Sweden

[3] Biopool AB, S-90347 Umea, Sweden

[4] Umea Univ, Dept Organ Chem, S-90187 Umea, Sweden

[5] Univ So Stockholm, Ctr Struct Biochem, Novum, S-14157 Huddinge, Sweden

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2004年 / 340卷 / 02期

关键词：

protein folding; hydrogen exchange; protein stability; intermediate; partially unfolded;

D O I：

10.1016/j.jmb.2004.05.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

We have analysed the folding energy landscape of the 72 amino acid protein MerP by monitoring native state hydrogen exchange as a function of temperature in the range of 7-55 degreesC. The temperature dependence of the hydrogen exchange has allowed us to determine DeltaG, DeltaH and DeltaC(p) values for the conformational processes that permit hydrogen exchange. When studied with the traditional probes, fluorescence and CD, MerP appears to behave as a typical two-state protein, but the results from the hydrogen exchange analysis reveal a much more complex energy landscape. Analysis at the individual amino acid level show that exchange is allowed from an ensemble of partially unfolded structures (i.e. intermediates) in which the stabilities at the amino acid level form a broad distribution throughout the protein. The formation of partially unfolded structures might contribute to the unusually slow folding of MerP. (C) 2004 Elsevier Ltd. All rights reserved.

引用

页码：333 / 344

页数：12

共 49 条

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