Visualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprinting.

ABSTRACT: Radiolytic protein footprinting with a synchrotron source is used to reveal detailed structural changes that occur in the Ca(2+)-dependent activation of gelsolin. More than 80 discrete peptides segments within the structure, covering 95% of the sequence in the molecule, were examined by footprinting and mass spectrometry for their solvent accessibility as a function of Ca(2+) concentration in solution. Twenty-two of the peptides exhibited detectable oxidation; for seven the oxidation extent was seen to be Ca(2+) sensitive. Ca(2+)titration isotherms monitoring the oxidation within residues 49-72 (within subdomain S1), 121-135 (S1), 162-166 (S2), and 722-748 (S6) indicate a three-state activation process with a intermediate that was populated at a Ca(2+) concentration of 1-5 microM that is c

SUBMITTER: Kiselar JG 

PROVIDER: S-EPMC153027 | biostudies-literature | 2003 Apr

REPOSITORIES: biostudies-literature