Abstract
Recent experiments involving single proteins have shown the importance of internal friction in protein dynamics. In addition to internal friction, solvent-quality also plays an important role in elucidating the structure and dynamics of proteins. Using a single chain based model where internal friction is introduced via dashpots between the neighbouring monomers and the solvent- quality is taken care of by introducing a mean field Flory type parameter, we monitor the effect of separation of two tagged monomers along the chain and the tail length on the reconfiguration time. We show that irrespective of the degree of compactness, the reconfiguration time remains unchanged beyond a tail length. Our calculations can also reproduce different trends observed in experiments.
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