A stabilized molten globule protein.

J Chang; A Bulychev; L Li

doi:10.1016/s0014-5793(00)02341-3

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PubMed · 11150528

A stabilized molten globule protein.

J Chang·A Bulychev·L Li

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Abstract

A predominant conformational isomer of non-native alpha-lactalbumin (alpha-LA) has been purified by thermal denaturation of the native alpha-LA using the technique of disulfide scrambling. This unique isomer retains a substantial content of alpha-helical structure. It is stabilized by two native disulfide bonds within the alpha-helical domain and two scrambled non-native disulfide bonds at the beta-sheet domain. This denatured isomer of alpha-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.

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Circular Dichroism Disulfides Drug Stability Hot Temperature Lactalbumin Models, Molecular Protein Conformation Protein Denaturation Protein Isoforms Protein Structure, Secondary Thermodynamics Journal Article Research Support, Non-U.S. Gov't

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J Chang, A Bulychev, L Li. 2000-12-29. A stabilized molten globule protein.. https://doi.org/10.1016/s0014-5793(00)02341-3

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