Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions.
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Structural, Bioinformatic, and In Vivo Analyses of Two Treponema pallidum Lipoproteins Reveal a Unique TRAP TransporterStructural and Thermodynamic Characterization of the Interaction between Two Periplasmic Treponema pallidum Lipoproteins that are Components of a TPR-Protein-Associated TRAP Transporter (TPAT)Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5Structure and Dynamics of Full-Length HIV-1 Capsid Protein in SolutionMulti-signal sedimentation velocity analysis with mass conservation for determining the stoichiometry of protein complexes.The boundary structure in the analysis of reversibly interacting systems by sedimentation velocity.Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT.Evaluating the stoichiometry of macromolecular complexes using multisignal sedimentation velocity.Trypanosoma brucei S-adenosylmethionine decarboxylase N terminus is essential for allosteric activation by the regulatory subunit prozymeOverview of current methods in sedimentation velocity and sedimentation equilibrium analytical ultracentrifugation.Analytical Ultracentrifugation as a Tool for Studying Protein Interactions.Tubulin Dimer Reversible Dissociation: AFFINITY, KINETICS, AND DEMONSTRATION OF A STABLE MONOMER.Recorded scan times can limit the accuracy of sedimentation coefficients in analytical ultracentrifugation.Multipoint binding of the SLP-76 SH2 domain to ADAP is critical for oligomerization of SLP-76 signaling complexes in stimulated T cells.Effect of arginine on oligomerization and stability of N-acetylglutamate synthaseIdentification of a core sequence for the binding of BosR to the rpoS promoter region in Borrelia burgdorferi.Protein-protein interactions: switch from classical methods to proteomics and bioinformatics-based approaches.Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.Sedimentation of Reversibly Interacting Macromolecules with Changes in Fluorescence Quantum Yield.Preferential assembly of heteromeric kainate and AMPA receptor amino terminal domains.
P2860
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P2860
Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions.
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
Using Lamm-Equation modeling o ...... f macromolecular interactions.
@ast
Using Lamm-Equation modeling o ...... f macromolecular interactions.
@en
type
label
Using Lamm-Equation modeling o ...... f macromolecular interactions.
@ast
Using Lamm-Equation modeling o ...... f macromolecular interactions.
@en
prefLabel
Using Lamm-Equation modeling o ...... f macromolecular interactions.
@ast
Using Lamm-Equation modeling o ...... f macromolecular interactions.
@en
P2860
P1433
P1476
Using Lamm-Equation modeling o ...... f macromolecular interactions.
@en
P2860
P356
10.1016/J.YMETH.2010.12.029
P577
2010-12-25T00:00:00Z