A stabilized molten globule protein

FEBS Letters

Chang, Jui-Yoa¹  Li, Li¹  Bulychev, Alexey¹ 

[1] Research Center for Protein Chemistry, Institute of Molecular Medicine and the Department of Biochemistry and Molecular Biology, University of Texas, 2121 W. Holcombe Blvd., Houston, TX 77030, USA

关键词: α-Lactalbumin;    Thermal denaturation;    Unfolding;    Unfolding intermediate;    Molten globule;    Scrambled α-lactalbumin;   

DOI  :  10.1016/S0014-5793(00)02341-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A predominant conformational isomer of non-native α-lactalbumin (α-LA) has been purified by thermal denaturation of the native α-LA using the technique of disulfide scrambling. This unique isomer retains a substantial content of α-helical structure. It is stabilized by two native disulfide bonds within the α-helical domain and two scrambled non-native disulfide bonds at the β-sheet domain. This denatured isomer of α-LA exhibits structural characteristics that are consistent with the well-documented molten globule state. The ability to prepare a stabilized and structurally defined molten globule provides a useful model for studying the folding and unfolding pathways of proteins.

【 授权许可】

Unknown