What can solid state NMR contribute to our understanding of protein folding?

ABSTRACT: Complete understanding of the folding process that connects a structurally disordered state of a protein to an ordered, biochemically functional state requires detailed characterization of intermediate structural states with high resolution and site specificity. While the intrinsically inhomogeneous and dynamic nature of unfolded and partially folded states limits the efficacy of traditional X-ray diffraction and solution NMR in structural studies, solid state NMR methods applied to frozen solutions can circumvent the complications due to molecular motions and conformational exchange encountered in unfolded and partially folded states. Moreover, solid state NMR methods can provide both qualitative and quantitative structural information at the site-specific level, even in the presence of s

SUBMITTER: Hu KN 

PROVIDER: S-EPMC2906680 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature