The alpha-helix folds on the millisecond time scale.

ABSTRACT: It has long been believed that nucleation of the alpha-helix is a very fast reaction, occurring in around 10(-7) s. We show here that helix nucleation, in fact, takes place on the millisecond time scale. The rate of alpha-helix nucleation in two polyalanine-based peptides and in lysine and glutamic acid homopolymers was measured directly by stopped-flow deep UV CD with synchrotron radiation as the light source. Synchrotron radiation CD gives far superior signal to noise than a conventional instrument. The 16-aa AK peptide folds with first-order kinetics and a rate constant of 15 s-1 at 0 degrees C. The rate-determining step is presumably the initiation of a new helix, which occurs at least 10(5) times slower than expected. Helix folding occurs in at least two steps on the millisecond time

SUBMITTER: Clarke DT 

PROVIDER: S-EPMC22062 | biostudies-literature | 1999 Jun

REPOSITORIES: biostudies-literature