Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy.

ABSTRACT: By using a Raman microscope, we show that it is possible to probe the conformational states in protein crystals and crystal fragments under growth conditions (in hanging drops). The flavin cofactor in the enzyme para-hydroxybenzoate hydroxylase can assume two conformations: buried in the protein matrix ("in") or essentially solvent-exposed ("out"). By using Raman difference spectroscopy, we previously have identified characteristic flavin marker bands for the in and out conformers in the solution phase. Now we show that the flavin Raman bands can be used to probe these conformational states in crystals, permitting a comparison between solution and crystal environments. The in or out marker bands are similar for the respective conformers in the crystal and in solution; however, significant

SUBMITTER: Altose MD 

PROVIDER: S-EPMC30597 | biostudies-literature | 2001 Mar

REPOSITORIES: biostudies-literature