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Biochemistry. 1994 Mar 1;33(8):2136-41.

A protein dissection study of a molten globule.

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  • 1Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge 02142.


Proteins have many distinct tertiary folds (Richardson, J. S. (1981) Adv. Prot. Chem. 34, 167-339). The term tertiary fold refers to the spatial organization of secondary structure elements (alpha-helices and beta-strands). It is not known when, in the process of protein folding, a native tertiary fold emerges. Here, we show that the helical domain of human alpha-lactalbumin, in isolation, forms a molten globule with the same overall tertiary fold as that found in intact alpha-lactalbumin. Formation of this native-like fold does not require extensive, specific side-chain packing. Our results suggest that much of the information transfer from one-dimension to three-dimensions has occurred at the molten globule stage of protein folding.

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