Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins.

ABSTRACT: Nuclear spin relaxation is a powerful method for studying molecular dynamics at atomic resolution. Recent methods development in biomolecular NMR spectroscopy has enabled detailed investigations of molecular dynamics that are critical for biological function, with prominent examples addressing allostery, enzyme catalysis, and protein folding. Dynamic processes with similar correlation times are often detected in multiple locations of the molecule, raising the question of whether the underlying motions are correlated (corresponding to concerted fluctuations involving many atoms distributed across extended regions of the molecule) or uncorrelated (corresponding to independent fluctuations involving few atoms in localized regions). Here, we have used (13)C(alpha)(i - 1)/(13)C(alpha)(i) differ

SUBMITTER: Lundstrom P 

PROVIDER: S-EPMC1287973 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature