Proton NMR spectroscopic studies of calcium-binding proteins. 2. Histidine microenvironments in .alpha.- and .beta.-parvalbumins as determined by protonation and laser photochemically induced dynamic nuclear polarization effects-Reference-Cited by-同舟云学术

Proton NMR spectroscopic studies of calcium-binding proteins. 2. Histidine microenvironments in .alpha.- and .beta.-parvalbumins as determined by protonation and laser photochemically induced dynamic nuclear polarization effects

Published:1986-04-08 Issue:7 Volume:25 Page:1826-1834
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Williams Thomas C.,Corson David C.,McCubbin William D.,Oikawa Kimio,Kay Cyril M.,Sykes Brian D.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00355a056

Reference42 articles.

1. Stepwise binding of small molecules to proteins. Nuclear magnetic resonance and temperature jump studies of the binding of 4-(N-acetylaminoglucosyl)-N-acetylglucosamine to lysozyme

2. Multinuclear NMR characterization of two coexisting conformational states of the Lactobacillus casei dihydrofolate reductase-trimethoprim-NADP complex

3. Ionization constants and thermodynamic parameters of histidine and derivatives

4. Assignment of proton NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy-, and (carbon monoxy)myoglobins

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