Native-state hydrogen-exchange studies of a fragment complex can provide structural information about the isolated fragments.

ABSTRACT: Ordered protein complexes are often formed from partially ordered fragments that are difficult to structurally characterize by conventional NMR and crystallographic techniques. We show that concentration-dependent hydrogen exchange studies of a fragment complex can provide structural information about the solution structures of the isolated fragments. This general methodology can be applied to any bimolecular or multimeric system. The experimental system used here consists of Ribonuclease S, a complex of two fragments of Ribonuclease A. Ribonuclease S and Ribonuclease A have identical three-dimensional structures but exhibit significant differences in their dynamics and stability. We show that the apparent large dynamic differences between Ribonuclease A and Ribonuclease S are caused by sm

SUBMITTER: Chakshusmathi G 

PROVIDER: S-EPMC22159 | biostudies-literature | 1999 Jul

REPOSITORIES: biostudies-literature