Revealing conformational substates of lipidated N-Ras protein by pressure modulation.

ABSTRACT: Regulation of protein function is often linked to a conformational switch triggered by chemical or physical signals. To evaluate such conformational changes and to elucidate the underlying molecular mechanisms of subsequent protein function, experimental identification of conformational substates and characterization of conformational equilibria are mandatory. We apply pressure modulation in combination with FTIR spectroscopy to reveal equilibria between spectroscopically resolved substates of the lipidated signaling protein N-Ras. Pressure has the advantage that its thermodynamic conjugate is volume, a parameter that is directly related to structure. The conformational dynamics of N-Ras in its different nucleotide binding states in the absence and presence of a model biomembrane was probe

SUBMITTER: Kapoor S 

PROVIDER: S-EPMC3258604 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature