Combined use of NMR relaxation measurements and hydrodynamic calculations to study protein association. Evidence for tetramers of low molecular weight protein tyrosine phosphatase in solution.
about
NMRDyn: a program for NMR relaxation studies of protein association.Protein tyrosine phosphatases: structure-function relationships.Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions.Protein loop compaction and the origin of the effect of arginine and glutamic acid mixtures on solubility, stability and transient oligomerization of proteinsStructure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions
P2860
Combined use of NMR relaxation measurements and hydrodynamic calculations to study protein association. Evidence for tetramers of low molecular weight protein tyrosine phosphatase in solution.
description
2003 nî lūn-bûn
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2003年の論文
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2003年学术文章
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name
Combined use of NMR relaxation ...... osine phosphatase in solution.
@en
Combined use of NMR relaxation ...... osine phosphatase in solution.
@nl
type
label
Combined use of NMR relaxation ...... osine phosphatase in solution.
@en
Combined use of NMR relaxation ...... osine phosphatase in solution.
@nl
prefLabel
Combined use of NMR relaxation ...... osine phosphatase in solution.
@en
Combined use of NMR relaxation ...... osine phosphatase in solution.
@nl
P2093
P356
P1476
Combined use of NMR relaxation ...... osine phosphatase in solution.
@en
P2093
Mikael Akke
Pau Bernadó
Tomas Akerud
P304
P356
10.1021/JA027836H
P407
P577
2003-01-01T00:00:00Z