Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.

ABSTRACT: Much of our knowledge of protein binding pathways is derived from extremely stable complexes that interact very tightly, with lifetimes of hours to days. Much less is known about weaker interactions and transient complexes because these are challenging to characterize experimentally. Nevertheless, these types of interactions are ubiquitous in living systems. The combination of NMR relaxation dispersion Carr-Purcell-Meiboom-Gill (CPMG) experiments and isothermal titration calorimetry allows the quantification of rapid binding kinetics for complexes with submillisecond lifetimes that are difficult to study using conventional techniques. We have used this approach to investigate the binding pathway of the Src homology 3 (SH3) domain from the Fyn tyrosine kinase, which forms complexes with pep

SUBMITTER: Meneses E 

PROVIDER: S-EPMC4183824 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature