Non-ideality by sedimentation velocity of halophilic malate dehydrogenase in complex solvents.
about
Modern analytical ultracentrifugation in protein science: a tutorial reviewTwo classes of bacterial IMPDHs according to their quaternary structures and catalytic propertiesProbing the conformation of FhaC with small-angle neutron scattering and molecular modeling.On the acquisition and analysis of microscale thermophoresis data.Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions.Structure and interactions of fish type III antifreeze protein in solution.Structural variation in human apolipoprotein E3 and E4: secondary structure, tertiary structure, and size distribution.Modelling non-homogeneous stochastic reaction-diffusion systems: the case study of gemcitabine-treated non-small cell lung cancer growthMacromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation.The use of analytical sedimentation velocity to extract thermodynamic linkage.Binding of alkyl polyglucoside surfactants to bacteriorhodopsin and its relation to protein stability.Role of analytical ultracentrifugation in assessing the aggregation of protein biopharmaceuticals.Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.Ion-specific modulation of protein interactions: anion-induced, reversible oligomerization of a fusion protein.The cytoplasmic domain of the T-cell receptor zeta subunit does not form disordered dimers.Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation.Electro-optical properties characterization of fish type III antifreeze protein.Allowance for radial dilution in evaluating the concentration dependence of sedimentation coefficients for globular proteins.Allowance for boundary sharpening in the determination of diffusion coefficients by sedimentation velocity: a historical perspective.Brownian dynamics simulations of analytical ultracentrifugation experiments exhibiting hydrodynamic and thermodynamic non-ideality.Concentration dependence of translational diffusion coefficients for globular proteins.Analytical ultracentrifugation: sedimentation velocity analysis.Dynamics of single polyelectrolyte chains in salt-free dilute solutions investigated by analytical ultracentrifugation.Measuring macromolecular size distributions and interactions at high concentrations by sedimentation velocity
P2860
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P2860
Non-ideality by sedimentation velocity of halophilic malate dehydrogenase in complex solvents.
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Non-ideality by sedimentation ...... ydrogenase in complex solvents
@nl
Non-ideality by sedimentation ...... drogenase in complex solvents.
@ast
Non-ideality by sedimentation ...... drogenase in complex solvents.
@en
type
label
Non-ideality by sedimentation ...... ydrogenase in complex solvents
@nl
Non-ideality by sedimentation ...... drogenase in complex solvents.
@ast
Non-ideality by sedimentation ...... drogenase in complex solvents.
@en
prefLabel
Non-ideality by sedimentation ...... ydrogenase in complex solvents
@nl
Non-ideality by sedimentation ...... drogenase in complex solvents.
@ast
Non-ideality by sedimentation ...... drogenase in complex solvents.
@en
P2093
P2860
P1433
P1476
Non-ideality by sedimentation ...... drogenase in complex solvents.
@en
P2093
P2860
P304
P356
10.1016/S0006-3495(01)75838-9
P407
P577
2001-10-01T00:00:00Z