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Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules
Published on: July 25, 2013
Forces contributing to the conformational stability of proteins
C N Pace1, B A Shirley, M McNutt
1Department of Medical Biochemistry and Genetics, Texas A&M University, College Station 77843-1114, USA.
Summary
For decades, scientists believed the hydrophobic effect was key to protein folding. New research shows hydrogen bonding and the hydrophobic effect contribute comparably to protein stability.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- The hydrophobic effect has long been considered the primary driver of protein folding.
- The net contribution of hydrogen bonding to protein stability remained unclear for decades.
Purpose of the Study:
- To re-evaluate the forces governing protein folding and stability.
- To clarify the role of hydrogen bonding in stabilizing globular proteins.
Main Methods:
- Analysis of mutant proteins.
- Comparative assessment of stabilizing forces.
Main Results:
- Studies on mutant proteins provided new insights into protein stabilization.
- Both hydrogen bonding and the hydrophobic effect contribute significantly to globular protein stability.
Conclusions:
- The hydrophobic effect and hydrogen bonding are major, comparable forces in protein stability.
- This finding challenges the long-held view of the hydrophobic effect as the sole dominant force.
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