Effects of Fluorination on the Folding Kinetics of a Heterodimeric Coiled Coil

被引：21

作者：

Salwiczek, Mario ^{[1
]}

Koksch, Beate ^{[1
]}

机构：

[1] Free Univ Berlin, Dept Biol Chem & Pharm, D-14195 Berlin, Germany

来源：

CHEMBIOCHEM | 2009年 / 10卷 / 18期

关键词：

alpha-helical coiled coil; fluorine; kinetics; non-natural amino acids; surface plasmon resonance; LEUCINE-ZIPPER; PROTEIN;

D O I：

10.1002/cbic.200900518

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 fast and the fluorous: SPR is a powerful method to investigate fast interactions between peptides and proteins. Differences of even one fluorine atom within a side chain can be detected. It is shown that fluorination of a single residue within the hydrophobic core results in a twofold increase in the association rate of a coiled-coil heterodimer. The observations furthermore reinvigorate the question whether fluorine-fluorine contacts in the unfolded state affect the kinetics of folding. © 2009 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：2867 / 2870

页数：4

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