Ligand Binding Constants to Lithium Hexamethyldisilazide Determined by Diffusion-Ordered NMR Spectroscopy

2017 ◽  
Vol 82 (12) ◽  
pp. 6223-6231 ◽  
Author(s):  
Onkei Tai ◽  
Russell Hopson ◽  
Paul G. Williard
Keyword(s):  
Nmr Spectroscopy ◽  
Ligand Binding ◽  
Binding Constants ◽  
Lithium Hexamethyldisilazide

scholarly journals Comprehensive Characterisation of the Ketoprofen-β-Cyclodextrin Inclusion Complex Using X-ray Techniques and NMR Spectroscopy

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 4089
Author(s):  
Katarzyna Betlejewska-Kielak ◽  
Elżbieta Bednarek ◽  
Armand Budzianowski ◽  
Katarzyna Michalska ◽  
Jan K. Maurin
Keyword(s):  
Nmr Spectroscopy ◽  
Inclusion Complex ◽  
Crystal And Molecular Structure ◽  
Binding Constants ◽  
Nmr Studies ◽  
X Ray ◽  
Cyclodextrin Inclusion ◽  
Powder Samples ◽  
Cyclodextrin Inclusion Complex ◽  
Co Precipitation

Racemic ketoprofen (KP) and β-cyclodextrin (β-CD) powder samples from co-precipitation (1), evaporation (2), and heating-under-reflux (3) were analysed using X-ray techniques and nuclear magnetic resonance (NMR) spectroscopy. On the basis of NMR studies carried out in an aqueous solution, it was found that in the samples obtained by methods 1 and 2, there were large excesses of β-CD in relation to KP, 10 and 75 times, respectively, while the sample obtained by method 3 contained equimolar amounts of β-CD and KP. NMR results indicated that KP/β-CD inclusion complexes were formed and the estimated binding constants were approximately 2400 M−1, showing that KP is quite strongly associated with β-CD. On the other hand, the X-ray single-crystal technique in the solid state revealed that the (S)-KP/β-CD inclusion complex with a stoichiometry of 2:2 was obtained as a result of heating-under-reflux, for which the crystal and molecular structure were examined. Among the methods used for the preparation of the KP/β-CD complex, only method 3 is suitable.

Uncertainty in protein–ligand binding constants: asymmetric confidence intervals versus standard errors

2021 ◽  
Author(s):  
Vaida Paketurytė ◽  
Vytautas Petrauskas ◽  
Asta Zubrienė ◽  
Olga Abian ◽  
Margarida Bastos ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Confidence Intervals ◽  
Binding Constants ◽  
Standard Errors

Determination of Substrate/Ligand Binding Constants from Electromotrive Force Measurements

2008 ◽  
Vol 37 (4) ◽  
pp. 519-526 ◽  
Author(s):  
M. Lopez-Lopez ◽  
P. Lopez-Cornejo ◽  
A. García ◽  
F. Sanchez
Keyword(s):  
Ligand Binding ◽  
Binding Constants ◽  
Force Measurements

The determination of axial ligand binding constants for iron porphyrins by cyclic voltammetry

1991 ◽  
Vol 68 (4) ◽  
pp. 337 ◽  
Author(s):  
David K. Geiger ◽  
Edmund J. Paviak ◽  
Lawrence T. Kass
Keyword(s):  
Cyclic Voltammetry ◽  
Ligand Binding ◽  
Binding Constants ◽  
Axial Ligand ◽  
Iron Porphyrins

scholarly journals Unpicking allosteric mechanisms of homo-oligomeric proteins by determining their successive ligand binding constants

2018 ◽  
Vol 373 (1749) ◽  
pp. 20170176 ◽  
Author(s):  
Ranit Gruber ◽  
Amnon Horovitz
Keyword(s):  
Mass Spectrometry ◽  
Ligand Binding ◽  
Single Molecule ◽  
Binding Constants ◽  
Molecular Machines ◽  
Native Mass Spectrometry ◽  
Oligomeric Proteins ◽  
Allosteric Mechanisms ◽  
The Relationship

Advances in native mass spectrometry and single-molecule techniques have made it possible in recent years to determine the values of successive ligand binding constants for large multi-subunit proteins. Given these values, it is possible to distinguish between different allosteric mechanisms and, thus, obtain insights into how various bio-molecular machines work. Here, we describe for ring-shaped homo-oligomers, in particular, how the relationship between the values of successive ligand binding constants is diagnostic for concerted, sequential and probabilistic allosteric mechanisms. This article is part of a discussion meeting issue ‘Allostery and molecular machines’.

Tritium NMR spectroscopy of ligand binding to maltose-binding protein

Biochemistry ◽  
1991 ◽  
Vol 30 (22) ◽  
pp. 5524-5531 ◽  
Author(s):  
Kalle Gehring ◽  
Philip G. Williams ◽  
Jeffrey G. Pelton ◽  
Hiromi Morimoto ◽  
David E. Wemmer
Keyword(s):  
Nmr Spectroscopy ◽  
Ligand Binding ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Tritium Nmr
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