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Hua Deng

Researcher at City University of New York

Publications -  39
Citations -  911

Hua Deng is an academic researcher from City University of New York. The author has contributed to research in topics: Raman spectroscopy & Cofactor. The author has an hindex of 19, co-authored 37 publications receiving 875 citations. Previous affiliations of Hua Deng include Albert Einstein College of Medicine.

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Nonresonance Raman Difference Spectroscopy: A General Probe of Protein Structure, Ligand Binding, Enzymatic Catalysis, and the Structures of Other Biomacromolecules

TL;DR: The author revealed that the Raman Difference Spectrometer was used in studies for the first time in the 1970s, and had shown promise in predicting the size and sources of error in the aftermath of the Chernobyl disaster.
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Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: a resonance Raman study of the Schiff base hydrogen/deuterium exchange

TL;DR: There are two anomalous results, the inconsistency of the observed hydrogen exchange rates of retinal Schiff base in the two pigments with those predicted from the standard exchange schemes and the enhancement of the rate of hydrogen exchange in the the two proteins over the model Schiffbase in aqueous solution.
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Classical Raman spectroscopic studies of NADH and NAD+ bound to liver alcohol dehydrogenase by difference techniques

TL;DR: The Raman spectra of reduced and oxidized nicotinamide adenine dinucleotide (NADH and NAD+, respectively) and adenosine 5'-diphosphate ribose (ADPR) when bound to the coenzyme site of liver alcohol dehydrogenase (LADH) are reported and the validity of the suggestion that theAdenine ring is protonated upon binding is discussed.
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A study of the Schiff base mode in bovine rhodopsin and bathorhodopsin

TL;DR: A force field is developed that accurately fits the observed ethylenic and protonated Schiff base stretching frequencies of rhodopsin and labeled derivatives and suggests that models for the efficient conversion of light to chemical energy in the r Rhodopsin to bathorhodopin photoconversion based solely on salt bridge separation of the protonate Schiff base and its counterion are probably incorrect.