Modulation of folding kinetics of repeat proteins: interplay between intra- and interdomain interactions.

ABSTRACT: Repeat proteins have unique elongated structures that, unlike globular proteins, are quite modular. Despite their simple one-dimensional structure, repeat proteins exhibit intricate folding behavior with a complexity similar to that of globular proteins. Therefore, repeat proteins allow one to quantify fundamental aspects of the biophysics of protein folding. One important feature of repeat proteins is the interfaces between the repeating units. In particular, the distribution of stabilities within and between the repeats was previously suggested to affect their folding characteristics. In this study, we explore how the interface affects folding kinetics and cooperativity by investigating two families of repeat proteins, namely, the Ankyrin and tetratricopeptide repeat proteins, which diff

SUBMITTER: Hagai T 

PROVIDER: S-EPMC3471457 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature