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A stabilized molten globule protein
Author(s) -
Chang Jui-Yoa,
Bulychev Alexey,
Li Li
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)02341-3
Subject(s) - molten globule , chemistry , native state , protein folding , crystallography , denaturation (fissile materials) , disulfide bond , folding (dsp implementation) , protein secondary structure , protein structure , beta sheet , alpha lactalbumin , stereochemistry , lactalbumin , circular dichroism , biochemistry , electrical engineering , nuclear chemistry , engineering
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.