Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes.

ABSTRACT: The time scale for ordering of the polypeptide backbone relative to the side chains is a critical issue in protein folding. The interplay between ordering of the backbone and ordering of the side chains is particularly important for the formation of β-sheet structures, as the polypeptide chain searches for the native stabilizing cross-strand interactions. We have studied these issues in the N-terminal domain of protein L9 (NTL9), a model protein with mixed α/β structure. We have developed a general approach for introducing site-specific IR probes for the side chains (azide) and backbone ((13)C═(18)O) using recombinant protein expression. Temperature-jump time-resolved IR spectroscopy combined with site-specific labeling enables independent measurement of the respective backbone and side-ch

SUBMITTER: Nagarajan S 

PROVIDER: S-EPMC3241911 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature