Measurement of Protein−Ligand Binding Constants from Reaction-Diffusion Concentration Profiles

Protein−ligand dissociation constants, K d, are determined precisely and down to the picomolar range from reaction-diffusion (RD) concentration profiles created by proteins diffusing through hydrogels functionalized with protein ligands. The RD process effectively amplifies the molecular-scale bindi...

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Veröffentlicht in:Analytical chemistry (Washington) 2010-11, Vol.82 (21), p.8780-8784
Hauptverfasser: Wei, Yanhu, Wesson, Paul J, Kourkine, Igor, Grzybowski, Bartosz A
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Wesson, Paul J
Kourkine, Igor
Grzybowski, Bartosz A
description Protein−ligand dissociation constants, K d, are determined precisely and down to the picomolar range from reaction-diffusion (RD) concentration profiles created by proteins diffusing through hydrogels functionalized with protein ligands. The RD process effectively amplifies the molecular-scale binding events into macroscopic patterns visible to the naked eye. The method is applicable to various protein−ligand pairs and does not require any prior knowledge about the protein structure.
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source MEDLINE; American Chemical Society Journals
subjects Analytical chemistry
Analytical, structural and metabolic biochemistry
Binding sites
Biological and medical sciences
Chemical reactions
Diffusion
Fundamental and applied biological sciences. Psychology
Gels - chemistry
Kinetics
Ligands
Measurement
Protein Binding
Proteins
Proteins - metabolism
title Measurement of Protein−Ligand Binding Constants from Reaction-Diffusion Concentration Profiles
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