Preferential interactions determine protein solubility in three-component solutions: the MgCl2 system.
about
The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.Steric exclusion is the principal source of the preferential hydration of proteins in the presence of polyethylene glycolsIon cooperativity and the effect of salts on polypeptide structure--a molecular dynamics study of BBA5 in salt solutions.Serge Timasheff: the man with a genius for solutions in biology.Solubility and aggregation of Gly(5) in water.Fluctuations and the Hofmeister effect.Structured disorder and conformational selection.Osmolyte-driven contraction of a random coil protein.A calorimetric characterization of the salt dependence of the stability of the GCN4 leucine zipperA mechanistic analysis of the increase in the thermal stability of proteins in aqueous carboxylic acid salt solutions.Patterns of protein protein interactions in salt solutions and implications for protein crystallization.Thermostabilization of inactivated polio vaccine in PLGA-based microspheres for pulsatile release.Identification of Protein-Excipient Interaction Hotspots Using Computational Approaches.Simulations of a protein crystal: explicit treatment of crystallization conditions links theory and experiment in the streptavidin-biotin complex.In vitro assessment of choline dihydrogen phosphate (CDHP) as a vehicle for recombinant human interleukin-2 (rhIL-2).Destabilization of Surfactant-Dispersed Carbon Nanotubes by Anions.A sparse matrix approach to the solubilization of overexpressed proteins.Solution nonideality related to solute molecular characteristics of amino acids.Molten globule and native state ensemble of Helicobacter pylori flavodoxin: can crowding, osmolytes or cofactors stabilize the native conformation relative to the molten globule?Protein-protein and protein-salt interactions in aqueous protein solutions containing concentrated electrolytes.Preformulation development of recombinant pegylated staphylokinase SY161 using statistical designCharacterization of highly concentrated antibody solution - A toolbox for the description of protein long-term solution stabilityA single Gly114Arg mutation stabilizes the hexameric subunit assembly and changes the substrate specificity of halo-archaeal nucleoside diphosphate kinase.Effect of cadmium acetate on the conformation of lysozyme: functional implications.Hydration shells with a pinch of salt.Protein-protein interactions in concentrated electrolyte solutions.Osmotic second virial cross-coefficient measurements for binary combination of lysozyme, ovalbumin, and α-amylase in salt solutions.
P2860
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P2860
Preferential interactions determine protein solubility in three-component solutions: the MgCl2 system.
description
1990 nî lūn-bûn
@nan
1990 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年学术文章
@wuu
1990年学术文章
@zh-cn
1990年学术文章
@zh-hans
1990年学术文章
@zh-my
1990年学术文章
@zh-sg
1990年學術文章
@yue
name
Preferential interactions dete ...... t solutions: the MgCl2 system.
@ast
Preferential interactions dete ...... t solutions: the MgCl2 system.
@en
type
label
Preferential interactions dete ...... t solutions: the MgCl2 system.
@ast
Preferential interactions dete ...... t solutions: the MgCl2 system.
@en
prefLabel
Preferential interactions dete ...... t solutions: the MgCl2 system.
@ast
Preferential interactions dete ...... t solutions: the MgCl2 system.
@en
P2093
P356
P1433
P1476
Preferential interactions dete ...... t solutions: the MgCl2 system.
@en
P2093
P304
P356
10.1021/BI00459A036
P407
P577
1990-02-01T00:00:00Z