THERMODYNAMICS OF α-HELIX FORMATION

被引:40
作者
Makhatadze, George I. [1 ]
机构
[1] Penn State Coll Med, Dept Biochem & Mol Biol, Hershey, PA 17033 USA
来源
PEPTIDE SOLVATION AND H-BONDS | 2005年 / 72卷
基金
美国国家卫生研究院;
关键词
D O I
10.1016/S0065-3233(05)72008-8
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 alpha-helix was the first proposed and experimentally confirmed secondary structure. The elegant simplicity of the alpha-helical structure, stabilized by hydrogen bonding between the backbone carbonyl oxygen and the peptide amide four residues away, has captivated the scientific community. In proteins, alpha-helices are also stabilized by the so-called capping interactions that occur at both the C- and the N-termini of the helix. This chapter provides a brief historical overview of the thermodynamic studies of the energetics of helix formation, and reviews recent progress in our understanding of the thermodynamics of helix formation.
引用
收藏
页码:199 / 226
页数:28
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