Ontology highlight
ABSTRACT:
SUBMITTER: Rimmerman D
PROVIDER: S-EPMC5804350 | biostudies-literature | 2017 Sep
REPOSITORIES: biostudies-literature
Rimmerman Dolev D Leshchev Denis D Hsu Darren J DJ Hong Jiyun J Kosheleva Irina I Chen Lin X LX
The journal of physical chemistry letters 20170905 18
Biological functions frequently require protein-protein interactions that involve secondary and tertiary structural perturbation. Here we study protein-protein dissociation and reassociation dynamics in insulin, a model system for protein oligomerization. Insulin dimer dissociation into monomers was induced by a nanosecond temperature-jump (T-jump) of ∼8 °C in aqueous solution, and the resulting protein and solvent dynamics were tracked by time-resolved X-ray solution scattering (TRXSS) on time ...[more]