Recorded scan times can limit the accuracy of sedimentation coefficients in analytical ultracentrifugation.
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Structural basis for activation and non-canonical catalysis of the Rap GTPase activating protein domain of plexinComplexes of neutralizing and non-neutralizing affinity matured Fabs with a mimetic of the internal trimeric coiled-coil of HIV-1 gp41MCM ring hexamerization is a prerequisite for DNA-binding.Crystal structure of the DdrB/ssDNA complex from Deinococcus radiodurans reveals a DNA binding surface involving higher-order oligomeric statesStructure and Dynamics of Full-Length HIV-1 Capsid Protein in SolutionIs Transthyretin a Regulator of Ubc9 SUMOylation?Computing translational diffusion and sedimentation coefficients: an evaluation of experimental data and programs.Improved measurement of the rotor temperature in analytical ultracentrifugation.Measurement of the temperature of the resting rotor in analytical ultracentrifugation.Analysis of high affinity self-association by fluorescence optical sedimentation velocity analytical ultracentrifugation of labeled proteins: opportunities and limitations.Dissociation of glucocerebrosidase dimer in solution by its co-factor, saposin C.A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation.Thermodynamic Interrogation of the Assembly of a Viral Genome Packaging Motor Complex.Variable Field Analytical Ultracentrifugation: II. Gravitational Sweep Sedimentation Velocity.Biochemical Roles for Conserved Residues in the Bacterial Fatty Acid-binding Protein Family.Improving the thermal, radial, and temporal accuracy of the analytical ultracentrifuge through external referencesStructural basis of recognition of farnesylated and methylated KRAS4b by PDEδ.Solution properties of γ-crystallins: compact structure and low frictional ratio are conserved properties of diverse γ-crystallins.Solution properties of γ-crystallins: hydration of fish and mammal γ-crystallins.Human herpesvirus 7 U21 tetramerizes to associate with class I major histocompatibility complex molecules.Analysis of protein interactions with picomolar binding affinity by fluorescence-detected sedimentation velocity.Use of fluorescence-detected sedimentation velocity to study high-affinity protein interactions.Dissection of specific binding of HIV-1 Gag to the 'packaging signal' in viral RNA.Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.Biochemical characterization of molybdenum cofactor-free nitrate reductase from Neurospora crassa.Biophysical and Structural Characterization of the Centriolar Protein Cep104 Interaction NetworkMolecular basis of CENP-C association with the CENP-A nucleosome at yeast centromeres.Structural basis of katanin p60:p80 complex formation.Effect of calcium ions on structure and stability of the C1q-like domain of otolin-1 from human and zebrafish.Structural Basis for Substrate Recognition by the Ankyrin Repeat Domain of Human DHHC17 Palmitoyltransferase.Dimeric and tetrameric forms of muscle fructose-1,6-bisphosphatase play different roles in the cell.Examination of the dynamic assembly equilibrium for E. coli ClpB.Measuring macromolecular size distributions and interactions at high concentrations by sedimentation velocity
P2860
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P2860
Recorded scan times can limit the accuracy of sedimentation coefficients in analytical ultracentrifugation.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Recorded scan times can limit ...... nalytical ultracentrifugation.
@en
type
label
Recorded scan times can limit ...... nalytical ultracentrifugation.
@en
prefLabel
Recorded scan times can limit ...... nalytical ultracentrifugation.
@en
P2093
P2860
P356
P1476
Recorded scan times can limit ...... nalytical ultracentrifugation.
@en
P2093
Grzegorz Piszczek
Huaying Zhao
Peter Schuck
Rodolfo Ghirlando
P2860
P304
P356
10.1016/J.AB.2013.02.011
P407
P577
2013-02-28T00:00:00Z