scholarly journals 19F NMR spectroscopy monitors ligand binding to recombinantly fluorine-labelled b′x from human protein disulphide isomerase (hPDI)

2014 ◽  
Vol 12 (23) ◽  
pp. 3808-3812 ◽  
Author(s):  
Rose Curtis-Marof ◽  
Denisa Doko ◽  
Michelle L. Rowe ◽  
Kirsty L. Richards ◽  
Richard A. Williamson ◽  
...  
Keyword(s):  
Nmr Spectroscopy ◽  
Recombinant Protein ◽  
Ligand Binding ◽  
Dissociation Constant ◽  
Human Protein ◽  
19F Nmr ◽  
Protein Disulphide Isomerase ◽  
Protein Labelling ◽  
Nmr Study ◽  
Constant Determination

Fluoroindole recombinant protein labelling enables a 19F NMR study to observe protein–ligand binding and dissociation constant determination.

scholarly journals Attractant- and Disulfide-Induced Conformational Changes in the Ligand Binding Domain of the Chemotaxis Aspartate Receptor: A 19F NMR Study

Biochemistry ◽  
1994 ◽  
Vol 33 (20) ◽  
pp. 6100-6109 ◽  
Author(s):  
Mark A. Danielson ◽  
Hans-Peter Biemann ◽  
Daniel E. Koshland ◽  
Joseph J. Falke
Keyword(s):  
Ligand Binding ◽  
Conformational Changes ◽  
Binding Domain ◽  
Ligand Binding Domain ◽  
19F Nmr ◽  
Aspartate Receptor ◽  
Nmr Study

scholarly journals 19F NMR study of ligand dynamics in carboxylate-bridged diiron(ii) complexes supported by a macrocyclic ligand

2015 ◽  
Vol 44 (41) ◽  
pp. 18111-18121 ◽  
Author(s):  
Mikael A. Minier ◽  
Stephen J. Lippard
Keyword(s):  
Nmr Spectroscopy ◽  
Macrocyclic Ligand ◽  
19F Nmr ◽  
Intramolecular Dynamics ◽  
Nmr Study

Using VT 19F NMR spectroscopy, we explored the intramolecular dynamics of a family of carboxylate-bridged diiron(ii) complexes, [Fe2(X2PIM)(ArRCCO2)2]. The data are consistent with these complexes undergoing μ–η1:η2 to μ–η1:η1 carboxylate shifts.

scholarly journals The ligand-binding b′ domain of human protein disulphide-isomerase mediates homodimerization

2009 ◽  
Vol 18 (12) ◽  
pp. 2569-2577 ◽  
Author(s):  
Anne Katrine Wallis ◽  
Ateesh Sidhu ◽  
Lee J. Byrne ◽  
Mark J. Howard ◽  
Lloyd W. Ruddock ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Human Protein ◽  
Protein Disulphide Isomerase

scholarly journals Tautomerisation in 1-(4-Methylphenylazo)naphthalen-2-ol and 2-(4-Methylphenylazo)-4-methylphenol: A Crystallographic and 13C{1H}NMR Study

1999 ◽  
Vol 23 (3) ◽  
pp. 178-179
Author(s):  
Wendy I. Cross ◽  
Kevin R. Flower ◽  
Robin G. Pritchard
Keyword(s):  
Acetic Acid ◽  
Nmr Spectroscopy ◽  
Resonant Frequency ◽  
X Ray Diffraction ◽  
X Ray ◽  
H Nmr ◽  
Nmr Study ◽  
Acetic Acid Esters ◽  
Acid Esters ◽  
Equivalent Carbon

The acetic acid esters of 1-(4-methylphenylazo)naphthalen-2-ol 1 and 2-(4-methylphenylazo)-4-methylphenol 3 are prepared and characterised by single crystal X-ray diffraction studies and 13C{1H}NMR spectroscopy; the position of the C(2)13C resonance for the ester is used to predict the position of resonant frequency of the equivalent carbon in the parent alcohols and hence, calculate the position of the azo-hydrazone equilibrium in these compounds.

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