Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.

ABSTRACT: Photochemically induced dynamic nuclear polarization NMR pulse-labeling techniques have been used to obtain detailed information about side-chain surface accessibilities in the partially folded (molten globule) states of bovine and human alpha-lactalbumin prepared under a variety of well defined conditions. Pulse labeling involves generating nuclear polarization in the partially folded state, rapidly refolding the protein within the NMR sample tube, then detecting the polarization in the well dispersed native-state spectrum. Differences in the solvent accessibility of specific side chains in the various molten globule states indicate that the hydrophobic clusters involved in stabilizing the alpha-lactalbumin fold can be formed from interactions between a variety of different hydrophobic re

SUBMITTER: Mok KH 

PROVIDER: S-EPMC1157025 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature