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A protein dissection study of a molten globule
1Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Department of Biology, Massachusetts Institute of Technology, Cambridge 02142.
Biochemistry
|March 1, 1994
Summary
Human alpha-lactalbumin
Area of Science:
- Biochemistry
- Structural Biology
- Protein Science
Background:
- Proteins fold into specific three-dimensional tertiary structures.
- The exact stage at which the native tertiary fold forms during protein folding is unknown.
Purpose of the Study:
- To investigate the protein folding process.
- To determine when the native tertiary fold emerges during protein folding.
Main Methods:
- Studied the helical domain of human alpha-lactalbumin in isolation.
- Analyzed the tertiary fold formation in the isolated domain.
Main Results:
- The isolated helical domain of human alpha-lactalbumin forms a molten globule.
- This molten globule exhibits the same tertiary fold as intact alpha-lactalbumin.
- Extensive side-chain packing is not necessary for forming this native-like fold.
Conclusions:
- The molten globule stage may represent a significant phase in protein folding.
- Much of the one-dimensional to three-dimensional information transfer occurs at the molten globule stage.