The high-resolution NMR structure of the early folding intermediate of the Thermus thermophilus ribonuclease H.

ABSTRACT: Elucidation of the high-resolution structures of folding intermediates is a necessary but difficult step toward the ultimate understanding of the mechanism of protein folding. Here, using hydrogen-exchange-directed protein engineering, we populated the folding intermediate of the Thermus thermophilus ribonuclease H, which forms before the rate-limiting transition state, by removing the unfolded regions of the intermediate, including an alpha-helix and two beta-strands (51 folded residues). Using multidimensional NMR, we solved the structure of this intermediate mimic to an atomic resolution (backbone rmsd, 0.51 A). It has a native-like backbone topology and shows some local deviations from the native structure, revealing that the structure of the folded region of an early folding intermedi

SUBMITTER: Zhou Z 

PROVIDER: S-EPMC2628467 | biostudies-literature | 2008 Dec

REPOSITORIES: biostudies-literature