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Fast Folding Dynamics of Small Proteins: Placing Limits on Diffusional Limits
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    SPEAKER(S)

Dr. Stephen Hagen - University of Florida, USA

Dr. Hagen received his PhD in physics at Princeton University and carried out postdoctoral studies in condensed matter physics at the University of Maryland. He then joined the Laboratory of Chemical Physics at the National Institutes of Health as a Staff Fellow where he worked with William Eaton on laser spectroscopic studies of protein conformational dynamics and folding. In 1999, Dr. Hagen joined the faculty of the Physics Department of the University of Florida. Dr. Hagen is interested in the rapid early stages of protein folding. His research group applies a variety of fast time-resolved techniques, including laser temperature-jump spectroscopy, transient absorbance spectroscopy and ultra fast mixing, to study fast events in folding. The primary focus is on understanding how the simplest physical properties of polypeptide chains control the rapid reconfiguration dynamics that occur early in the folding process.

Talk Online Publication: Oct 2007

TOPICS COVERED IN FAST FOLDING DYNAMICS OF SMALL PROTEINS: PLACING LIMITS ON DIFFUSIONAL LIMITS

Basic time scales and diffusional limits in protein folding - Applying reaction rate theories to folding - Kramers behavior and friction - Internal friction of polymer chains - Evidence for (or against) internal friction in protein folding - Fast folding experiments and methodology - Interpretations: internal time scales versus internal viscosity - Limitations of the "diffusional limits" picture

How to cite this talk:
Hagen, S. (2007), "Fast Folding Dynamics of Small Proteins: Placing Limits on Diffusional Limits", in Wright, C. (ed.), Protein Folding, Aggregation and Design: Concepts, Experiments, Theories and Mechanisms, The Biomedical & Life Sciences Collection, Henry Stewart Talks Ltd, London (online at http://hstalks.com/bio)

Direct talk access link:
http://hstalks.com/lib.php?t=HST3.1106_1_2&c=252

    DETAILED SLIDE INDEX

1. Introduction
2. Some basic time scales in folding (1)
3. Loop formation times
4. Chain relaxation times
5. Some basic time scales in folding (2)
6. Folding as a unimolecular reaction
7. Classical transition state theory (TST)
8. Folding is diffusion-controlled
9. Diffusion driven barrier-crossing
10. Kramers behavior in folding simulations
11. Viscosity dependence of DNA hairpin closure
12. Folding: is friction due to solvent alone?
13. Solvent viscosity and peptide loop formation
14. Internal friction and polymer dynamics
15. Internal friction due to backbone rotations
16. Internal friction in conformational dynamics
17. Viscosity effects in protein folding
18. Other complications in viscosity studies
19. Internal friction in folding? (I)
20. Internal friction in folding? (2)
21. Internal friction in folding? (3)
22. Preparing a "friction-limited" system
23. Laser-triggered folding kinetics
24. Folding time vs. solvent viscosity
25. Comparing two IF experiments
26. Reaction-coordinate dependent diffusion constant
27. Large activation energy for t-0
28. Tryptophan Cage (Tc5b)
29. Viscosity dependence at constant delta G
30. TrpCage k-f and k-u
31. Compare to k-f simulations
32. Limiting folding/unfolding times
33. Conclusions
34. Acknowledgments
35. END