Structure and flexibility within proteins as identified through small angle X-ray scattering.

ABSTRACT: Flexibility between domains of proteins is often critical for function. These motions and proteins with large scale flexibility in general are often not readily amenable to conventional structural analysis such as X-ray crystallography, nuclear magnetic resonance spectroscopy (NMR) or electron microscopy. A common evolution of a crystallography project, once a high resolution structure has been determined, is to postulate possible sights of flexibility. Here we describe an analysis tool using relatively inexpensive small angle X-ray scattering (SAXS) measurements to identify flexibility and validate a constructed minimal ensemble of models, which represent highly populated conformations in solution. The resolution of these results is sufficient to address the questions being asked: what ki

SUBMITTER: Pelikan M 

PROVIDER: S-EPMC3773563 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature