Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography.

ABSTRACT: Steric constraints, charged interactions and many other forces important to protein structure and function can be explored by mutagenic experiments. Research of this kind has led to a wealth of knowledge about what stabilizes proteins in their folded states. To gain a more complete picture requires that we perturb these structures in a continuous manner, something mutagenesis cannot achieve. With high pressure crystallographic methods it is now possible to explore the detailed properties of proteins while continuously varying thermodynamic parameters. Here, we detail the structural response of the cavity-containing mutant L99A of T4 lysozyme, as well as its pseudo wild-type (WT*) counterpart, to hydrostatic pressure. Surprisingly, the cavity has almost no effect on the pressure response: v

SUBMITTER: Collins MD 

PROVIDER: S-EPMC1853337 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature