Spatiotemporal correlations in denatured proteins: The dependence of fluorescence resonance energy transfer (FRET)-derived protein reconfiguration times on the location of the FRET probes

摘要: There has been considerable effort to understand the inherent time scale for conformational reconfiguration of denatured proteins. Even a simple homopolymer, however, exhibits spectrum fluctuation scales rather than unique characteristic time. Consequently, different may be probed by measurements. Motivated recent single-molecule fluorescence resonance energy transfer experiments, here I have studied theoretically how exhibited fluctuations distance between two residues within an unfolded polypeptide depends on choice residue pair. This was generally found become shorter as sequence separation is reduced. The maximum time, corresponds not being located at ends chain but each residing short length apart from ends. Comparison these findings with measurements suggests that latter bear signatures transient residual structure.