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Exploring the Dynamic Range of the Kinetic Exclusion Assay in. – A high unspecific binding response concealed the specific binding response when we used HBST as running buffer (a commonly used buffer in Biacore assays) in which we had studied DKK1 and DKK4. To minimize unspecific binding of our His-tagged DKK2, which had a theoretical net charge of +23 at pH 7.0, we chose a kosmotropic buffer, as used by other investigators when studying analytes with high pI values  .
PDF Unveiling the hidden structure of complex stochastic. – THE JOURNAL OF CHEMICAL PHYSICS 140, 064101 (2014) Unveiling the hidden structure of complex stochastic biochemical networks Angelo Valleriani,1,a) Xin Li,2 and Anatoly B. kolomeisky3 1max planck Institute of Colloids and Interfaces, Department of Theory and Bio-Systems, 14424 Potsdam, Germany
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Mad About Madtoms, by Don Orth – blogspot.com – Mad About Madtoms, by Don Orth In my last blog post, I explored the paradox of the popular, though venomous, little madtom (genus Noturus ). But there is more to the madtom story than that painful sting.
Conformational Dynamics Govern the Free-Energy Landscape of a. – (b) bimolecular quenching rate constant, k q, from time-resolved fluorescence quenching plotted against the number of carbon atoms in the detergent alkyl chain, n C. (c) Correlation time within 0-15 ns, cor, for dipolar relaxation versus n C, with data in OM, DM, DDM, and LDAO taken from reference .
Exploring the Dynamic Range of the Kinetic Exclusion Assay in. – The kinetic exclusion assay (KinExA) is a solution-based method to determine the concentrations of interacting binding partners and the equilibrium dissociation constants (KD) of biomolecular interactions, typically in the pM to low nM range.
Unveiling the hidden structure of complex stochastic. – THE JOURNAL OF CHEMICAL PHYSICS 140, 064101 (2014) Unveiling the hidden structure of complex stochastic biochemical networks Angelo Valleriani,1,a) Xin Li,2 and Anatoly B. Kolomeisky3 1Max Planck Institute of Colloids and Interfaces, Department of Theory and Bio-Systems, 14424 Potsdam, Germany
Direct Electrochemistry of Redox Enzymes as a Tool for. – In contrast, former models of "catalytic electrodes" assumed bimolecular reaction between catalyst and substrate and will be relevant to enzyme electrochemistry only for s < K m ( s is the concentration of substrate).