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Published on: July 16, 2017
Conformational dynamics and ensembles in protein folding
1Department of Chemistry and Biochemistry, University of Maryland, College Park, Maryland 20742, USA. vmunoz@umd.edu
Annual Review of Biophysics and Biomolecular Structure
|February 13, 2007
Summary
Recent advances in protein folding experiments enhance our understanding of polypeptide dynamics and folding pathways. Fast-folding proteins near the downhill folding regime offer new research avenues for resolving folding mechanisms and stabilizing interactions.
Area of Science:
- Biochemistry
- Biophysics
- Structural Biology
Background:
- Protein folding is a fundamental process in biology.
- Interpreting experimental data in protein folding has been historically challenging.
- Long-standing questions regarding protein folding mechanisms persist.
Purpose of the Study:
- To explore how recent experimental developments improve the interpretation of protein folding data.
- To connect experimental findings with theoretical models for a deeper understanding.
- To investigate the characteristics of fast-folding proteins and their implications.
Main Methods:
- Utilizing recent experimental developments in protein folding research.
- Employing a variety of independent methods to estimate folding barriers.
- Conducting structural and statistical analysis of global downhill folding.
Main Results:
- Experimental data interpretation in protein folding is improving, bridging theory and practice.
- A roadmap of relevant polypeptide motions and timescales for folding stages is emerging.
- Consistently small folding barriers suggest many fast-folding proteins are in the downhill folding regime.
- Global downhill folding analysis shows promise for resolving folding mechanisms and stabilizing interactions.
Conclusions:
- Fast-folding proteins near the downhill folding regime represent a significant area for future research.
- Equilibrium experiments on nonmutated proteins can directly resolve folding mechanisms.
- Understanding noncovalent interactions that stabilize native structures is facilitated by these new approaches.
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