Analysis of protein interactions with picomolar binding affinity by fluorescence-detected sedimentation velocity.
about
On the acquisition and analysis of microscale thermophoresis data.Analytical ultracentrifugation with fluorescence detection system reveals differences in complex formation between recombinant human TNF and different biological TNF antagonists in various environments.Accounting for photophysical processes and specific signal intensity changes in fluorescence-detected sedimentation velocityCombining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT.A multilaboratory comparison of calibration accuracy and the performance of external references in analytical ultracentrifugation.A histogram approach to the quality of fit in sedimentation velocity analyses.3D-Printing for Analytical UltracentrifugationTubulin Dimer Reversible Dissociation: AFFINITY, KINETICS, AND DEMONSTRATION OF A STABLE MONOMER.Higher-order oligomerization promotes localization of SPOP to liquid nuclear speckles.Monochromatic multicomponent fluorescence sedimentation velocity for the study of high-affinity protein interactions.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.Sedimentation velocity analytical ultracentrifugation for characterization of therapeutic antibodies.
P2860
Q31035661-5E4E9531-3BAB-4ACD-B481-EB5F2105FB86Q33641909-C68CBEEE-576A-44AC-A9AF-5745AA9003E3Q34193963-4AE50D23-4E12-4D17-9216-27D8EDBA05B7Q35006796-7073F752-5846-4F7B-A87A-DED1C9441C50Q35634385-177B0F5F-2F4F-49F4-ACE5-C18666D31BC4Q35706762-9E0E8625-1E25-45BC-AA05-4D4B9E0E94EBQ36104104-88241140-B5AF-43AD-942E-B4287D9BEA37Q36884861-2DD3B501-37AB-4307-9035-B19B08D1A3D6Q37011857-6573274E-CA4A-4531-B0AF-50444BAE6C36Q37175856-4DF5A457-6D34-4A31-9069-D2E7119DD793Q38644638-E0F7B152-D9F9-4D19-98CE-1F23CFBECE6FQ38840409-D7F8914C-C00E-452D-9B9E-765C8EEDCCE8Q47100457-E3FC7A2C-2D65-4596-A8FD-917A1B5E819BQ47247669-C3686ECD-4A06-411A-9CAD-5B168C076CDA
P2860
Analysis of protein interactions with picomolar binding affinity by fluorescence-detected sedimentation velocity.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 05 March 2014
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Analysis of protein interactio ...... tected sedimentation velocity.
@en
Analysis of protein interactio ...... tected sedimentation velocity.
@nl
type
label
Analysis of protein interactio ...... tected sedimentation velocity.
@en
Analysis of protein interactio ...... tected sedimentation velocity.
@nl
prefLabel
Analysis of protein interactio ...... tected sedimentation velocity.
@en
Analysis of protein interactio ...... tected sedimentation velocity.
@nl
P2860
P356
P1433
P1476
Analysis of protein interactio ...... tected sedimentation velocity.
@en
P2093
Huaying Zhao
Mark L Mayer
P2860
P304
P356
10.1021/AC500093M
P407
P50
P577
2014-03-05T00:00:00Z