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 |
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creator | Wei, Yanhu 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. |
doi_str_mv | 10.1021/ac102055a |
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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.</description><identifier>ISSN: 0003-2700</identifier><identifier>EISSN: 1520-6882</identifier><identifier>DOI: 10.1021/ac102055a</identifier><identifier>PMID: 20923152</identifier><identifier>CODEN: ANCHAM</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical chemistry ; Analytical, structural and metabolic biochemistry ; Binding sites ; Biological and medical sciences ; Chemical reactions ; Diffusion ; Fundamental and applied biological sciences. 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Chem</addtitle><date>2010-11-01</date><risdate>2010</risdate><volume>82</volume><issue>21</issue><spage>8780</spage><epage>8784</epage><pages>8780-8784</pages><issn>0003-2700</issn><eissn>1520-6882</eissn><coden>ANCHAM</coden><abstract>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.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>20923152</pmid><doi>10.1021/ac102055a</doi><tpages>5</tpages></addata></record> |
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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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