Competition between intramolecular and intermolecular interactions in an amyloid-forming protein.

ABSTRACT: Despite much progress in understanding the folding and the aggregation processes of proteins, the rules defining their interplay have yet to be fully defined. This problem is of particular importance since many diseases are initiated by protein unfolding and hence the propensity to aggregate competes with intramolecular collapse and other folding events. Here, we describe the roles of intramolecular and intermolecular interactions in defining the length of the lag time and the apparent rate of elongation of the 100-residue protein human beta(2)-microglobulin at pH 2.5, commencing from an acid-denatured state that lacks persistent structure but contains significant non-random hydrophobic interactions. Using a combination of site-directed mutagenesis, quantitative kinetic analysis and comput

SUBMITTER: Routledge KE 

PROVIDER: S-EPMC2722902 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature