Conformational changes in melittin upon complexation with an anionic melittin analog

FEBS Letters

Aimoto, Saburo²  Bello, Jake¹  Ramalingam, Kalaiyarasi¹ 

[1] Department of Chemistry, Roswell Park Division of the Graduate School, State University of New York at Buffalo, 666 Elm Street, Buffalo, NY 14263, USA;Institute for Protein Research, Osaka University, Suita City, Osaka 565, Japan

关键词: Melittin;    Anionic melittin analog;    Circular dichroism;    Conformation;    Melting profile;    Cold-denaturation;   

DOI  :  10.1016/0014-5793(91)81417-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Melittin and its Glu-(7,21,22,23,24) analog upon mixing in equimolar concentrations form a hybrid oligomer with significant helical structure, in conditions in which each peptide separately adopts a largely disordered structure. The hybrid exhibits both cold- and heat-induced denaturations similar to the phenomena exhibited by proteins. The hybrid also retains significant residual structure at higher temperature, similar to the ‘molten globular state’ that has been suggested for proteins. Melittin, at concentrations in which it forms helical tetramers, also exhibits these phenomena and may be used as a model for protein-denaturation studies.

【 授权许可】

Unknown