Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions.
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Charge matters.Selective and specific ion binding on proteins at physiologically-relevant concentrations.Specific ion effects on macromolecular interactions in Escherichia coli extracts.Protein Stabilization and Enzyme Activation in Ionic Liquids: Specific Ion EffectsHigh-throughput biophysical analysis of protein therapeutics to examine interrelationships between aggregate formation and conformational stability.Models and mechanisms of Hofmeister effects in electrolyte solutions, and colloid and protein systems revisited.Preferential interactions of trehalose, L-arginine.HCl and sodium chloride with therapeutically relevant IgG1 monoclonal antibodies.Optimizing the Bioavailability of Subcutaneously Administered Biotherapeutics Through Mechanochemical Drivers.The Charge Properties of Phospholipid NanodiscsSAXS/SANS on Supercharged Proteins Reveals Residue-Specific Modifications of the Hydration ShellRadar chart array analysis to visualize effects of formulation variables on IgG1 particle formation as measured by multiple analytical techniques.Mapping site-specific changes that affect stability of the N-terminal domain of calmodulin.Challenges in Predicting Protein-Protein Interactions from Measurements of Molecular DiffusivityCritical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.Bridging interactions of proteins with silica nanoparticles: the influence of pH, ionic strength and protein concentration.Ribosome surface properties may impose limits on the nature of the cytoplasmic proteome.Ion Specificity and Nonmonotonic Protein Solubility from Salt Entropy.Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Protein charge determination and implications for interactions in cell extracts.Concentration dependent viscosity of monoclonal antibody solutions: explaining experimental behavior in terms of molecular properties.Weak IgG self- and hetero-association characterized by fluorescence analytical ultracentrifugation.A postreductionist framework for protein biochemistry.
P2860
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P2860
Effective charge measurements reveal selective and preferential accumulation of anions, but not cations, at the protein surface in dilute salt solutions.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Effective charge measurements ...... face in dilute salt solutions.
@en
Effective charge measurements ...... face in dilute salt solutions.
@nl
type
label
Effective charge measurements ...... face in dilute salt solutions.
@en
Effective charge measurements ...... face in dilute salt solutions.
@nl
prefLabel
Effective charge measurements ...... face in dilute salt solutions.
@en
Effective charge measurements ...... face in dilute salt solutions.
@nl
P2093
P2860
P356
P1433
P1476
Effective charge measurements ...... face in dilute salt solutions.
@en
P2093
Atul Saluja
David N Brems
R Matthew Fesinmeyer
Susan F Chase
Thomas M Laue
Vladimir Razinkov
Yatin R Gokarn
P2860
P304
P356
10.1002/PRO.591
P577
2011-03-01T00:00:00Z