Characterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experiment.

ABSTRACT: Recent theoretical/computational studies based on simplified protein models and experimental investigation have suggested that the native structure of a protein plays a primary role in determining the folding rate and mechanism of relatively small single-domain proteins. Here, we extend the study of the relationship between protein topology and folding mechanism to a larger protein with complex topology, by analyzing the folding process of monomeric lactose repressor (MLAc) computationally by using a Gō-like C(alpha) model. Next, we combine simulation and experimental results (see companion article in this issue) to achieve a comprehensive assessment of the folding landscape of this protein. Remarkably, simulated kinetic and equilibrium analyses show an excellent quantitative agreement wit

SUBMITTER: Das P 

PROVIDER: S-EPMC1253569 | biostudies-literature | 2005 Oct

REPOSITORIES: biostudies-literature