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Updated: May 16, 2026
10:09
Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Molten globules, entropy-driven conformational change and protein folding
Robert L Baldwin1, George D Rose
1Department of Biochemistry, Stanford University Medical Center, Stanford, CA 94305-5307, United States. baldwinb@stanford.edu
Current Opinion in Structural Biology
|December 15, 2012
Summary
Molten globule proteins achieve specific binding without close-packed side chains, challenging established models of molecular recognition and protein folding. This suggests alternative mechanisms drive protein structure and function.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Dynamics
Background:
- Established models emphasize side chain close-packing for molecular recognition in protein folding and binding.
- Proteins can exhibit function even without this close-packing, suggesting alternative mechanisms.
Purpose of the Study:
- To challenge the paradigm that side chain close-packing is essential for protein function.
- To explore the role of alternative factors in molecular recognition and protein folding.
Main Methods:
- Analysis of molten globule and dry molten globule protein states.
- Comparison of protein structures and functions in the presence and absence of side chain close-packing.
Main Results:
- Molten globule proteins bind targets specifically despite lacking side chain close-packing.
- Dry molten globule states retain native topology but lack close-packing, admitting or excluding solvent.
Conclusions:
- Side chain close-packing is not the sole determinant of molecular recognition or protein function.
- Protein structure and function can be mediated by factors beyond intricate side chain arrangements.
- Established models of protein folding and binding require re-evaluation.
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