Domain cooperativity in multidomain proteins: what can we learn from molecular alignment in anisotropic media?

ABSTRACT: Many proteins have modular design with multiple globular domains connected via flexible linkers. As a simple model of such system, we study a tandem construct consisting of two identical SH3 domains and a variable-length Gly/Ser linker. When the linker is short, this construct represents a dumbbell-shaped molecule with limited amount of domain-domain mobility. Due to its elongated shape, this molecule efficiently aligns in steric alignment media. As the length of the linker increases, the two domains become effectively uncoupled and begin to behave as independent entities. Consequently, their degree of alignment drops, approaching that found in the (near-spherical) isolated SH3 domains. To model the dependence of alignment parameters on the length of the interdomain linker, we have generat

SUBMITTER: Yuwen T 

PROVIDER: S-EPMC4721247 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature