Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
about
Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein–protein complex structure determinationUsing MUSIC and CC(CO)NH for backbone assignment of two medium-sized proteins not fully accessible to standard 3D NMR.Resonance assignment of disordered protein with repetitive and overlapping sequence using combinatorial approach reveals initial structural propensities and local restrictions in the denatured state.Combination of ¹⁵N reverse labeling and afterglow spectroscopy for assigning membrane protein spectra by magic-angle-spinning solid-state NMR: application to the multidrug resistance protein EmrEResonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.Isotope labeling for solution and solid-state NMR spectroscopy of membrane proteinsRecent applications of isotopic labeling for protein NMR in drug discovery.Rapid NMR Assignments of Proteins by Using Optimized Combinatorial Selective Unlabeling.Hydrogen exchange of disordered proteins in Escherichia coli.Monitoring Ras Interactions with the Nucleotide Exchange Factor Son of Sevenless (Sos) Using Site-specific NMR Reporter Signals and Intrinsic Fluorescence.Stable isotope labeling strategy based on coding theory.Phosphorylation-dependent changes in nucleotide binding, conformation, and dynamics of the first nucleotide binding domain (NBD1) of the sulfonylurea receptor 2B (SUR2B).Solution NMR characterization of apical membrane antigen 1 and small molecule interactions as a basis for designing new antimalarials.Bacterial production of site specific 13C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins.Production of Single-Chain Fv Antibodies Specific for GA-Pyridine, an Advanced Glycation End-Product (AGE), with Reduced Inter-Domain Motion.Current NMR Techniques for Structure-Based Drug Discovery.Efficient sequential assignments in proteins with reduced dimensionality 3D HN(CA)NH.Backbone H, C, and N resonance assignments of the ligand binding domain of the human wildtype glucocorticoid receptor and the F602S mutant variantLate metabolic precursors for selective aromatic residue labelingSelective isotope labelling of leucine residues by using α-ketoacid precursor compounds
P2860
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P2860
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
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年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
name
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@ast
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@en
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@nl
type
label
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@ast
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@en
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@nl
prefLabel
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@ast
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@en
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@nl
P2093
P2860
P1476
Amino acid selective unlabeling for sequence specific resonance assignments in proteins.
@en
P2093
Anushikha Thakur
B Krishnarjuna
Garima Jaipuria
Hanudatta S Atreya
Patrick D'Silva
P2860
P2888
P356
10.1007/S10858-010-9459-Z
P577
2010-12-09T00:00:00Z