Conformational Dynamics of the Partially Disordered Yeast Transcription Factor GCN4.

ABSTRACT: Molecular dynamics (MD) simulations have been employed to study the conformational dynamics of the partially disordered DNA binding basic leucine zipper domain of the yeast transcription factor GCN4. We demonstrate that back-calculated NMR chemical shifts and spin-relaxation data provide complementary probes of the structure and dynamics of disordered protein states and enable comparisons of the accuracy of multiple MD trajectories. In particular, back-calculated chemical shifts provide a sensitive probe of the populations of residual secondary structure elements and helix capping interactions, while spin-relaxation calculations are sensitive to a combination of dynamic and structural factors. Back calculated chemical shift and spin-relaxation data can be used to evaluate the populations o

SUBMITTER: Robustelli P 

PROVIDER: S-EPMC3882080 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature