A stabilized molten globule protein

Citations of this article
Mendeley users who have this article in their library.


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. © 2000 Federation of European Biochemical Societies.




Chang, J. Y., Bulychev, A., & Li, L. (2000). A stabilized molten globule protein. FEBS Letters, 487(2), 298–300. https://doi.org/10.1016/S0014-5793(00)02341-3

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free