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We consider a phantom chain model of polymer with internal friction in aharmonic confinement and extend it to take care of effects of solvent qualityfollowing a mean field approach where an exponent $\nu$ is introduced. Themodel termed as "Solvent Dependent Compacted Rouse with Internal Friction(SDCRIF)" is then used to calculate the reconfiguration time of a chain thatrelates to recent F\"{o}rster resonance energy transfer (FRET) studies onfolded and intrinsically disordered proteins (IDPs) and can account for theeffects of solvent quality as well as the denaturant concentration on thereconfiguration dynamics. Following an ansatz that relates the strength of theharmonic confinement ($k_c$) with the internal friction of the chain($\xi_{int}$), SDCRIF can convincingly reproduce the experimental data andexplain how the denaturant can change the time scale for the internal friction.It can also predict near zero internal friction in case of IDPs. In addition,our calculations show that the looping time as well as the reconfiguration timescales with the chain length $N$ as $\sim N^\alpha$, where $\alpha$ dependsweakly on the internal friction but has rather stronger dependence on thesolvent quality. In absence of any internal friction, $\alpha=2\nu+1$ and itgoes down in presence of internal friction, but looping slows down in general.On the contrary, poorer the solvent, faster the chain reconfigures and formsloop, even though one expects high internal friction in the collapsed state.However, if the internal friction is too high then the looping andreconfiguration dynamics become slow even in poor solvent.

Reconfiguration Dynamics in folded and intrinsically disordered protein with internal friction: Effect of solvent quality and denaturant