scholarly journals Determination of Effector Binding Affinities Using Photoacoustic Calorimetry

2018 ◽  
Vol 114 (3) ◽  
pp. 416a
Author(s):  
Jovany J. Betancourt ◽  
Jaroslava Miksovska
Keyword(s):  
Binding Affinities ◽  
Photoacoustic Calorimetry ◽  
Effector Binding

scholarly journals Recognition of hydrogen isotopomers by an open-cage fullerene

2013 ◽  
Vol 371 (1998) ◽  
pp. 20110629 ◽  
Author(s):  
Yasujiro Murata ◽  
Shih-Ching Chuang ◽  
Fumiyuki Tanabe ◽  
Michihisa Murata ◽  
Koichi Komatsu
Keyword(s):  
Equilibrium Constants ◽  
Equilibrium Mixture ◽  
Size Difference ◽  
Binding Affinities ◽  
Kinetic Isotope ◽  
Molecular Sizes ◽  
Lower Temperature ◽  
Kinetics Of ◽  
Pressure Hydrogen

We present our study on the recognition of hydrogen isotopes by an open-cage fullerene through determination of binding affinity of isotopes H 2 /HD/D 2 with the open-cage fullerene and comparison of their relative molecular sizes through kinetic-isotope-release experiments. We took advantage of isotope H 2 /D 2 exchange that generated an equilibrium mixture of H 2 /HD/D 2 in a stainless steel autoclave to conduct high-pressure hydrogen insertion into an open-cage fullerene. The equilibrium constants of three isotopes with the open-cage fullerene were determined at various pressures and temperatures. Our results show a higher equilibrium constant for HD into open-cage fullerene than the other two isotopomers, which is consistent with its dipolar nature. D 2 molecule generally binds stronger than H 2 because of its heavier mass; however, the affinity for H 2 becomes larger than D 2 at lower temperature, when size effect becomes dominant. We further investigated the kinetics of H 2 /HD/D 2 release from open-cage fullerene, proving their relative escaping rates. D 2 was found to be the smallest and H 2 the largest molecule. This notion has not only supported the observed inversion of relative binding affinities between H 2 and D 2 , but also demonstrated that comparison of size difference of single molecules through non-convalent kinetic-isotope effect was applicable.

A Reference Scale of Cucurbit[7]uril Binding Affinities

2021 ◽  
Author(s):  
Mohammad A. Alnajjar ◽  
Werner M Nau ◽  
Andreas Hennig
Keyword(s):  
Accurate Determination ◽  
Binding Affinities ◽  
High Binding ◽  
Reference Scale ◽  
Direct Binding ◽  
Guest Chemistry

The accurate determination of ultra-high binding affinities in supramolecular host-guest chemistry is a challenging endeavour because direct binding titrations are generally limited to affinities <106 M-1 due to sensitivity constraints...

Electrophoretic affinity measurements on microchip. Determination of binding affinities between diketopiperazine receptors and peptide ligands

2007 ◽  
Vol 28 (11) ◽  
pp. 1832-1838 ◽  
Author(s):  
Alexandra R. Stettler ◽  
Philipp Krattiger ◽  
Helma Wennemers ◽  
Maria A. Schwarz
Keyword(s):  
Peptide Ligands ◽  
Binding Affinities

scholarly journals Determination of the range in binding-site densities of rat skin heparin chains with high binding affinities for antithrombin

1988 ◽  
Vol 251 (1) ◽  
pp. 141-145 ◽  
Author(s):  
A A Horner ◽  
M Kusche ◽  
U Lindahl ◽  
C B Peterson
Keyword(s):  
Chemical Analysis ◽  
Binding Site ◽  
Binding Affinity ◽  
Intrinsic Fluorescence ◽  
Binding Affinities ◽  
Rat Skin ◽  
High Binding ◽  
Site Density ◽  
High Binding Affinity

Rat skin heparin proteoglycans vary markedly in the proportions of their constituent polysaccharide chains that have high binding affinity for antithrombin. As the proportion of such chains in a proteoglycan rises, their degree of affinity for antithrombin also increases [Horner (1987) Biochem. J. 244, 693-698]. The antithrombin-binding-site densities of such chains have now been determined, by measuring heparin-induced enhancement of the intrinsic fluorescence of antithrombin and by chemical analysis for the disaccharide sequence glucuronosyl-N-sulphoglucosaminyl (3,6-di-O-sulphate), which is unique to this site in heparin [Lindahl, Bäckström, Thunberg & Leder (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6551-6555]. Antithrombin-binding-site density ranged from one to five sites per chain.

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