Raman crystallography and other biochemical applications of Raman microscopy.
Recent studies using a Raman microscope have shown that single protein crystals provide an ideal platform to undertake Raman difference spectroscopic analyses under nonresonance conditions. This approach, termed Raman crystallography, provides a means of characterizing chemical events within the crystal such as ligand binding and enzyme reactions. In many cases Raman crystallography goes hand in hand with X-ray crystallographic studies because the Raman results can inform the X-ray crystallographer about the status of chemical events in the crystal prior to flash freezing and X-ray analysis. In turn, the combined data from the Raman and X-ray analyses are highly synergistic and offer novel perspectives on structure and dynamics in enzyme active sites. In a related area, protein misfolding, Raman microscopy can provide detailed insights into the chemistry of the amyloid plaques associated with Alzheimer's disease and into the intermediates on the alpha-synuclein protein misfolding pathway implicated in Parkinson's disease.
Carey
Paul R
PR
Department of Biochemistry, Case Western Reserve University, Cleveland, Ohio 44106, USA. paul.carey@case.edu
D015109:4-Hydroxybenzoate-3-Monooxygenase / Q000737:chemistry; D016229:Amyloid beta-Peptides / Q000737:chemistry; D019878:Carboxyl and Carbamoyl Transferases / Q000737:chemistry; D003461:Crystallography / Q000379:methods*; D006801:Humans; D008853:Microscopy / Q000379:methods*; D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry*; D013059:Spectrum Analysis, Raman / Q000379:methods*; D051844:alpha-Synuclein / Q000737:chemistry; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000737:chemistry
D016229:Amyloid beta-Peptides; D011506:Proteins; D051844:alpha-Synuclein; D065093:beta-Lactamase Inhibitors; D015109:4-Hydroxybenzoate-3-Monooxygenase; D019878:Carboxyl and Carbamoyl Transferases; C021580:Methylmalonyl-CoA carboxytransferase; D001618:beta-Lactamases