Conformations of diphosphopyridine coenzymes upon binding to dehydrogenases (Q35104789)

6 August 2017

title

Conformations of diphosphopyridine coenzymes upon binding to dehydrogenases (English)

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6 August 2017

Lee CY

1

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6 August 2017

Eichner RD

series ordinal

2

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6 August 2017

Kaplan NO

series ordinal

3

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6 August 2017

language of work or name

English

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publication date

1 May 1973

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Proceedings of the National Academy of Sciences of the United States of America

6 August 2017

published in

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6 August 2017

volume

70

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6 August 2017

issue

5

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6 August 2017

page(s)

1593-1597

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Enzyme-substrate interaction by nuclear magnetic resonance

6 August 2017

cites work

1 reference

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Nuclear magnetic resonance studies of the structure and binding sites of enzymes. IV. Cytidine 3'-monophosphate binding to ribonuclease

9 July 2018

1 reference

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Assignment of the histidine peaks in the nuclear magnetic resonance spectrum of ribonuclease

9 July 2018

1 reference

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220 MHz proton nuclear magnetic resonance study of the interaction between chicken M4 lactate dehydrogenase and reduced diphosphopyridine nucleotide

9 July 2018

1 reference

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Some effects of environment on the folding of nicotinamide-adenine dinucleotides in aqueous solutions

9 July 2018

1 reference

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A structure of pyridine nucleotides in solution

9 July 2018

1 reference

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Lactate dehydrogenase of lobster (Homarus americanus) tail muscle. II. Kinetics and regulatory properties.

9 July 2018

1 reference

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A Proton Magnetic Resonance Study of the Association of Lysozyme with Monosaccharide Inhibitors

9 July 2018

1 reference

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The conformation of pyridine dinucleotides in solution

27 September 2018

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12 December 2020

The comparative enzymology of lactic dehydrogenases. 3. Properties of the H4 and M4 enzymes from a number of vertebrates

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12 December 2020

Interaction between lysozyme and acetamido sugars as detected by proton magnetic resonance spectroscopy

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12 December 2020

A nuclear magnetic resonance study of substrate binding by alcohol dehydrogenases

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12 December 2020

A nuclear magnetic resonance study of association equilibrium and enzyme-bound environments of N-acetyl-D-glucosamine anomers and lysozyme

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12 December 2020

Application of transient nuclear magnetic resonance methods to the measurement of biological exchange rates. Interaction of trifluoroacetyl-D-phenylalanine with the chymotrypsins

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12 December 2020

Nuclear magnetic resonance studies of the interaction of trans-cinnamate with .alpha.-chymotrypsin

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12 December 2020

Nuclear magnetic resonance studies of the structure and binding sites of enzymes. 8. Inhibitor binding to ribonuclease

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12 December 2020

A 31P NMR study of the association of uridine-3′-monophosphate to ribonuclease A

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12 December 2020

Fluorescence spectra and polarization of glyceraldehyde-3-phosphate and lactic dehydrogenase coenzyme complexes

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12 December 2020

Proton Magnetic Resonance Investigation of Enzyme–Coenzyme Complexes

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12 December 2020

Identifiers

DOI

10.1073/PNAS.70.5.1593

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6 August 2017

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6 August 2017

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