Structure and dynamics of protein waters revealed by radiolysis and mass spectrometry.

ABSTRACT: Water is critical for the structure, stability, and functions of macromolecules. Diffraction and NMR studies have revealed structure and dynamics of bound waters at atomic resolution. However, localizing the sites and measuring the dynamics of bound waters, particularly on timescales relevant to catalysis and macromolecular assembly, is quite challenging. Here we demonstrate two techniques: first, temperature-dependent radiolytic hydroxyl radical labeling with a mass spectrometry (MS)-based readout to identify sites of bulk and bound water interactions with surface and internal residue side chains, and second, H(2)(18)O radiolytic exchange coupled MS to measure the millisecond dynamics of bound water interactions with various internal residue side chains. Through an application of the meth

SUBMITTER: Gupta S 

PROVIDER: S-EPMC3443160 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature