The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State.

ABSTRACT: The N-terminal domain of L9 (NTL9) is a 56-residue mixed α-β protein that lacks disulfides, does not bind cofactors, and folds reversibly. NTL9 has been widely used as a model system for experimental and computational studies of protein folding and for investigations of the unfolded state. The role of side-chain interactions in the folding of NTL9 is probed by mutational analysis. ϕ-values, which represent the ratio of the change in the log of the folding rate upon mutation to the change in the log of the equilibrium constant for folding, are reported for 25 point mutations and 15 double mutants. All ϕ-values are small, with an average over all sites probed of only 0.19 and a largest value of 0.4. The effect of modulating unfolded-state interactions is studied by measuring ϕ-values in seco

SUBMITTER: Sato S 

PROVIDER: S-EPMC5425357 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature