Validation of response function construction and probing heterogeneous protein hydration by intrinsic tryptophan.

ABSTRACT: Protein solvation dynamics usually occur on multiple time scales with site specificity, and the characterization of such heterogeneous dynamics requires a convenient optical probe. We proposed a tryptophan methodology, and with site-directed mutagenesis we can use a tryptophan scan to probe any desirable position around protein surfaces. Here, we report our extended solvation model for construction of response functions for probes such as tryptophan with multiple emission peaks and lifetimes. We show our systematic construction procedure and careful analyses of the possible missing percentage of an initial ultrafast component with the established zero-time emission spectrum and limited temporal resolution through two methods of the direct mapping of femtosecond-resolved fluorescence spectr

SUBMITTER: Qin Y 

PROVIDER: S-EPMC3499651 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature