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10.1021/ac500094v http://scihub22266oqcxt.onion/10.1021/ac500094v C4238591!4238591!25314127     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Anal+Chem 2014 ; 86 (22): 11045-54 Nephropedia Template TP {{tp|p=25314127|t=2014. Determination of Multivalent Protein?Ligand Binding Kinetics by Second-Harmonic Correlation Spectroscopy |pdf=|usr=}}{{25314127}} gab.com Text Determination of Multivalent Protein Ligand Binding Kinetics by Second-Harmonic Correlation Spectroscopy JO: Anal Chem http://www.kidney.de/pget.php?&tw=1&pmid=25314127 #FOAvip Binding kinetics of the multivalent proteins peanut agglutinin (PnA) and cholera toxin B subunit (CTB) to a GM1-doped 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) lipid bilayer were investigated by both second-harmonic correlation spectroscopy (SHCS) and a traditional equilibrium binding isotherm. Adsorption and desorption rates, as well as binding affinity and binding free energy, for three bulk protein concentrations were determined by SHCS. For PnA binding to GM1, the measured adsorption rate decreased with increasing bulk PnA concentration from (3.7 ± 0.3) × 106 M?1·s?1 at 0.43 ?M PnA to (1.1 ± 0.1) × 105 M?1·s?1 at 12 ?M PnA. CTB?GM1 exhibited a similar trend, decreasing from (1.0 ± 0.1) × 109 M?1·s?1 at 0.5 nM CTB to (3.5 ± 0.2) × 106 M?1·s?1 at 240 nM CTB. The measured desorption rates in both studies did not exhibit any dependence on initial protein concentration. As such, 0.43 ?M PnA and 0.5 nM CTB had the strongest measured binding affinities, (3.7 ± 0.8) × 109 M?1 and (2.8 ± 0.5) × 1013 M?1, respectively. Analysis of the binding isotherm data suggests there is electrostatic repulsion between protein molecules when PnA binds GM1, while CTB?GM1 demonstrates positive ligand?ligand cooperativity. This study provides additional insight into the complex interactions between multivalent proteins and their ligands and showcases SHCS for examining these complex yet technologically important protein?ligand complexes used in biosensors, immunoassays, and other biomedical diagnostics. Twit Text FOAVip Determination of Multivalent Protein Ligand Binding Kinetics by Second-Harmonic Correlation Spectroscopy ????Anal Chem http://www.kidney.de/pget.php?&tw=1&pmid=25314127 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25314127 #FOAvip English Wikipedia <ref>{{Cite pmid|25314127}}</ref> Determination of Multivalent Protein?Ligand Binding Kinetics by Second-Harmonic Correlation Spectroscopy #MMPMID25314127 Sly K; Conboy JC Anal Chem 2014[Nov]; 86 (22): 11045-54 PMID25314127show ga Binding kinetics of the multivalent proteins peanut agglutinin (PnA) and cholera toxin B subunit (CTB) to a GM1-doped 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC) lipid bilayer were investigated by both second-harmonic correlation spectroscopy (SHCS) and a traditional equilibrium binding isotherm. Adsorption and desorption rates, as well as binding affinity and binding free energy, for three bulk protein concentrations were determined by SHCS. For PnA binding to GM1, the measured adsorption rate decreased with increasing bulk PnA concentration from (3.7 ± 0.3) × 106 M?1·s?1 at 0.43 ?M PnA to (1.1 ± 0.1) × 105 M?1·s?1 at 12 ?M PnA. CTB?GM1 exhibited a similar trend, decreasing from (1.0 ± 0.1) × 109 M?1·s?1 at 0.5 nM CTB to (3.5 ± 0.2) × 106 M?1·s?1 at 240 nM CTB. The measured desorption rates in both studies did not exhibit any dependence on initial protein concentration. As such, 0.43 ?M PnA and 0.5 nM CTB had the strongest measured binding affinities, (3.7 ± 0.8) × 109 M?1 and (2.8 ± 0.5) × 1013 M?1, respectively. Analysis of the binding isotherm data suggests there is electrostatic repulsion between protein molecules when PnA binds GM1, while CTB?GM1 demonstrates positive ligand?ligand cooperativity. This study provides additional insight into the complex interactions between multivalent proteins and their ligands and showcases SHCS for examining these complex yet technologically important protein?ligand complexes used in biosensors, immunoassays, and other biomedical diagnostics. äDetermination of Multivalent Protein?Ligand Binding Kinetics by Second(epmc).pdf DeepDyve Pubget Overpricing