Ultraviolet (239 nm) resonance Raman spectroscopy of an enzyme-substrate intermediate of papain
Author:
Publisher
Wiley
Subject
Spectroscopy,General Materials Science
Reference11 articles.
1. Resonance enhanced Raman identification of the zinc-oxygen bond in a horse liver alcohol dehydrogenase-nicotinamide adenine dinucleotide-aldehyde transient chemical intermediate
2. Resonance-enhanced Raman identification of a ternary chemical intermediate during the equine liver alcohol dehydrogenase reduction of p-(dimethylamino)benzaldehyde
3. Resonance Raman carbonyl frequencies and ultraviolet absorption maxima as indicators of the active site environment in native and unfolded chromophoric acyl-.alpha.-chymotrypsin
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5. Characterization of Transient Enzyme-Substrate Bonds by Resonance Raman Spectroscopy
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1. Raman spectroscopy as a probe of protein structure in food systems;Protein Structure-Function Relationships in Foods;1994
2. Ultraviolet resonance Raman spectra of pea intact, large, and small phytochromes: Differences in molecular topography of the red- and far-red-absorbing forms;Biochemistry;1993-07-01
3. Time-resolved UV resonance Raman study on Bohr effects of hemoglobin;Journal of the American Chemical Society;1992-04
4. UV Resonance Raman Studies of Bacteria;Applied Spectroscopy Reviews;1992-03
5. The Time Dependent UV Resonance Raman Spectra, Conformation, and Biological Activity of Acetylcholine Analogues Upon Binding to Acetylcholine Binding Proteins;Journal of Biomolecular Structure and Dynamics;1991-12
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