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Picosecond Protein Dynamics
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| Proteins are biological nano-machines. Each exhibits a distinctive structural design and performs specific biological function in living organisms. While a protein is carrying out its function, this nature-designed nano-machine undergoes a series of movements (so called functionally important structural dynamics). Each movement (structural transition) of a protein requires it to surmount an energy barrier along the reaction coordinate. Although the structures and the rates of structural transitions of various proteins have been extensively studied, important questions regarding what drives protein structural transitions remain poorly understood. We address the energetics of protein structural dynamics by studying the channels and mechanism of energy flow in proteins and in model systems and to investigate how selective vibrational excitations accelerate certain key protein structural transitions.
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Papers
R.H. Austin, S.S. Chan. (2003) Of spherical cows, cloudy crystal balls, and proteins. Biochem Biophys Res commun, 312(1):215-21.
G.S. Edwards, R.H. Austin, F.E. Carroll, M.L. Copeland, M.E. Couprie, W.E. Gabella, R.F. Haglund, B.A. Hooper, M.S. Hutson, E.D. Jansen, K.M. Joos, D.P. Kiehart, I. Lindau, J. Miao, H.S. Pratisto, J.H. Shen, Y. Tokutake, A.F.G. Meer, A. Xie. (2003) Free-electron-laser-based biophysical and biomedical instrumentation. Rev. Sci. Instrum, 74(7):3207-3245.
R.H. Austin, A. Xie, L. Meer, M. Shinn, G. Neil. (2003) Self-trapped states in proteins. Nuclear Instruments and Methods in Physical Research A, 507: 561-563
Robert H. Austin, Aihua Xie, Lees van der Meer, Michelle Shinn, George Neil, (2003), Self-trapped states in proteins. Journal of Physics: Condensed Matter. 15:S1693-S1698.
Olgica Bakajin, Thomas A. J. Duke, Jonas Tegenfeldt, Chia-Fu Chou, Shirley S. Chan, Robert H. Austin, and Edward C. Cox. Separation of 100 kilobase DNA molecules in 10 seconds. (2001) Anal. Chem. 73: 6053- 6057
H. Frauenfelder, B.H. McMahon, R.H. Austin, Kelvin Chu and John T. Groves (2001) The role of Structure, Energy Landscape, Dynamics and Allostery in the Enzymatic Function of Myoglobin, Proc. Natl. Acad. Sci. USA 98: 2370-2374
A. Xie, L. van der Meer, W. Hoff and R.H. Austin (2000) Long-Lived Amide I Vibrational Modes in Myoglobin, Physical Review Letters 84: 5435-5438
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