The analysis of macromolecular interactions by sedimentation equilibrium
about
Structure-Function Studies of DNA Binding Domain of Response Regulator KdpE Reveals Equal Affinity Interactions at DNA Half-SitesStructure and Dynamics of Full-Length HIV-1 Capsid Protein in SolutionComputing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs.On the acquisition and analysis of microscale thermophoresis data.Predicting Protein-protein Association Rates using Coarse-grained Simulation and Machine Learning.SEDFIT-MSTAR: molecular weight and molecular weight distribution analysis of polymers by sedimentation equilibrium in the ultracentrifuge.Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.Multi-signal sedimentation velocity analysis with mass conservation for determining the stoichiometry of protein complexes.Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT.Analysis of high-affinity assembly for AMPA receptor amino-terminal domains.Variable-Field Analytical Ultracentrifugation: I. Time-Optimized Sedimentation Equilibrium.Thermodynamic Interrogation of the Assembly of a Viral Genome Packaging Motor Complex.Quantitative characterization of temperature-independent and temperature-dependent protein-protein interactions in highly nonideal solutions.Biophysical characterization of membrane proteins in nanodiscs.Overview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.Analytical Ultracentrifugation as a Tool for Studying Protein Interactions.Protein-protein interactions: switch from classical methods to proteomics and bioinformatics-based approaches.Characterising protein/detergent complexes by triple-detection size-exclusion chromatography.Role of E2-RING Interactions in Governing RNF4-Mediated Substrate Ubiquitination.A structural organization for the Disrupted in Schizophrenia 1 protein, identified by high-throughput screening, reveals distinctly folded regions, which are bisected by mental illness-related mutations.
P2860
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P2860
The analysis of macromolecular interactions by sedimentation equilibrium
description
2010 nî lūn-bûn
@nan
2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The analysis of macromolecular interactions by sedimentation equilibrium
@ast
The analysis of macromolecular interactions by sedimentation equilibrium
@en
The analysis of macromolecular interactions by sedimentation equilibrium
@nl
type
label
The analysis of macromolecular interactions by sedimentation equilibrium
@ast
The analysis of macromolecular interactions by sedimentation equilibrium
@en
The analysis of macromolecular interactions by sedimentation equilibrium
@nl
prefLabel
The analysis of macromolecular interactions by sedimentation equilibrium
@ast
The analysis of macromolecular interactions by sedimentation equilibrium
@en
The analysis of macromolecular interactions by sedimentation equilibrium
@nl
P2860
P1433
P1476
The analysis of macromolecular interactions by sedimentation equilibrium
@en
P2093
Rodolfo Ghirlando
P2860
P304
P356
10.1016/J.YMETH.2010.12.005
P577
2010-12-16T00:00:00Z