Raman spectroscopic studies of the structures, energetics, and bond distortions of substrates bound to enzymes.
Deng
H
H
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Callender
R
R
D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000737:chemistry; D004798:Enzymes / Q000737:chemistry*; D005958:Glucosephosphates / Q000737:chemistry; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008968:Molecular Conformation; D009699:N-Glycosyl Hydrolases / Q000737:chemistry; D010710:Phosphates / Q000737:chemistry; D010733:Phosphoglucomutase / Q000737:chemistry; D011485:Protein Binding; D012697:Serine Endopeptidases / Q000737:chemistry; D013059:Spectrum Analysis, Raman / Q000295:instrumentation / Q000379:methods*; D013762:Tetrahydrofolate Dehydrogenase / Q000737:chemistry; D013816:Thermodynamics; D014638:Vanadates / Q000737:chemistry
D004791:Enzyme Inhibitors; D004798:Enzymes; D005958:Glucosephosphates; D010710:Phosphates; D014638:Vanadates; C031590:glucose-1-phosphate; D013762:Tetrahydrofolate Dehydrogenase; D009699:N-Glycosyl Hydrolases; C096466:inosine-uridine hydrolase; D012697:Serine Endopeptidases; D010733:Phosphoglucomutase