Revisiting the NMR structure of the ultrafast downhill folding protein gpW from bacteriophage λ.

ABSTRACT: GpW is a 68-residue protein from bacteriophage λ that participates in virus head morphogenesis. Previous NMR studies revealed a novel α+β fold for this protein. Recent experiments have shown that gpW folds in microseconds by crossing a marginal free energy barrier (i.e., downhill folding). These features make gpW a highly desirable target for further experimental and computational folding studies. As a step in that direction, we have re-determined the high-resolution structure of gpW by multidimensional NMR on a construct that eliminates the purification tags and unstructured C-terminal tail present in the prior study. In contrast to the previous work, we have obtained a full manual assignment and calculated the structure using only unambiguous distance restraints. This new structure confi

SUBMITTER: Sborgi L 

PROVIDER: S-EPMC3208555 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature