Arnab, Mukherjee and Biman, Bagchi (2003) Fluorescence resonance energy transfer dynamics during protein folding: Evidence of multistage folding kinetics. In: Current Science, 85 (1). pp. 68-72.
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Fluorescence resonance energy transfer (FRET) during folding of a model protein, HP-36, is investigated by Brownian dynamics simulation. Computer simulations of this protein show that folding kinetics is non-exponential and multistage, after a fast initial hydrophobic collapse. This multistage dynamics can be captured in FRET with a suitably chosen donor-acceptor pair. In particular, we find that FRET can be sensitive to late stages of changes in the radius of gyration which is found to occur for this model protein. This late stage dynamics is driven by changes in the topological pair contact formation.
|Item Type:||Journal Article|
|Additional Information:||Copyright of this article belongs to Indian Academy of Sciences.|
|Department/Centre:||Division of Chemical Sciences > Solid State & Structural Chemistry Unit|
|Date Deposited:||19 Apr 2007|
|Last Modified:||19 Sep 2010 04:37|
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