NMR structure determination and investigation using a reduced proton (REDPRO) labeling strategy for proteins
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Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy.Overview on the use of NMR to examine protein structure.Determination of ligand binding modes in weak protein-ligand complexes using sparse NMR data.Differential ubiquitin binding by the acidic loops of Ube2g1 and Ube2r1 enzymes distinguishes their Lys-48-ubiquitylation activities.Dependence of distance distributions derived from double electron-electron resonance pulsed EPR spectroscopy on pulse-sequence time.The complex binding mode of the peptide hormone H2 relaxin to its receptor RXFP1Fractional deuteration applied to biomolecular solid-state NMR spectroscopyQuantitative Determination of Interacting Protein Surfaces in Prokaryotes and Eukaryotes by Using In-Cell NMR Spectroscopy.Differential isotope-labeling for Leu and Val residues in a protein by E. coli cellular expression using stereo-specifically methyl labeled amino acids.
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P2860
NMR structure determination and investigation using a reduced proton (REDPRO) labeling strategy for proteins
description
im Juli 2002 veröffentlichter wissenschaftlicher Artikel
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scientific article published on 01 July 2002
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в липні 2002
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name
NMR structure determination an ...... labeling strategy for proteins
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NMR structure determination and investigation using a reduced proton
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type
label
NMR structure determination an ...... labeling strategy for proteins
@en
NMR structure determination and investigation using a reduced proton
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prefLabel
NMR structure determination an ...... labeling strategy for proteins
@en
NMR structure determination and investigation using a reduced proton
@nl
P2860
P921
P1433
P1476
NMR structure determination an ...... labeling strategy for proteins
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P2093
Michael Goger
Ranajeet Ghose
P2860
P304
P356
10.1016/S0014-5793(02)03051-X
P407
P577
2002-07-01T00:00:00Z