Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.
about
Phage-Induced Alignment of Membrane Proteins Enables the Measurement and Structural Analysis of Residual Dipolar Couplings with Dipolar Waves and λ-MapsImproved Cross Validation of a Static Ubiquitin Structure Derived from High Precision Residual Dipolar Couplings Measured in a Drug-Based Liquid Crystalline PhaseSpatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEsStereospecific assignments in proteins using exact NOEs.Self-consistent residual dipolar coupling based model-free analysis for the robust determination of nanosecond to microsecond protein dynamics.High accuracy of Karplus equations for relating three-bond J couplings to protein backbone torsion angles.Toward a unified representation of protein structural dynamics in solution.Residual dipolar couplings: are multiple independent alignments always possible?Influence of histidine tag attachment on picosecond protein dynamics.The use of residual dipolar coupling in studying proteins by NMR.Simultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences.MERA: a webserver for evaluating backbone torsion angle distributions in dynamic and disordered proteins from NMR data.Compiled data set of exact NOE distance limits, residual dipolar couplings and scalar couplings for the protein GB3Site-specific backbone amide (15)N chemical shift anisotropy tensors in a small protein from liquid crystal and cross-correlated relaxation measurements.Dynafold: a dynamic programming approach to protein backbone structure determination from minimal sets of Residual Dipolar Couplings.Efficient and accurate estimation of relative order tensors from lambda-mapsMeasurement of (1)H-(15)N and (1)H-(13)C residual dipolar couplings in nucleic acids from TROSY intensities.The impact of hydrogen bonding on amide 1H chemical shift anisotropy studied by cross-correlated relaxation and liquid crystal NMR spectroscopy.A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein.Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding propertiesSide Chain Conformational Distributions of a Small Protein Derived from Model-Free Analysis of a Large Set of Residual Dipolar CouplingsThe Exact NOE as an Alternative in Ensemble Structure Determination.Modulating alignment of membrane proteins in liquid-crystalline and oriented gel media by changing the size and charge of phospholipid bicelles.Protein backbone motions viewed by intraresidue and sequential HN-Halpha residual dipolar couplingsARTSY-J: Convenient and precise measurement of (3)JHNHα couplings in medium-size proteins from TROSY-HSQC spectra.NMR determination of amide N-H equilibrium bond length from concerted dipolar coupling measurements.Correlated dynamics between protein HN and HC bonds observed by NMR cross relaxation.Improved accuracy of 15N-1H scalar and residual dipolar couplings from gradient-enhanced IPAP-HSQC experiments on protonated proteins.Measuring dynamic and kinetic information in the previously inaccessible supra-τ(c) window of nanoseconds to microseconds by solution NMR spectroscopy.NMR studies of dynamic biomolecular conformational ensembles.ORIUM: optimized RDC-based Iterative and Unified Model-free analysisDirect Investigation of Slow Correlated Dynamics in Proteins via Dipolar Interactions.Cross-correlated relaxation rates between protein backbone H-X dipolar interactions.Detection of Correlated Protein Backbone and Side-Chain Angle Fluctuations.Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G.Microsecond Dynamics in Ubiquitin Probed by Solid-State 15 N NMR Spectroscopy R1ρ Relaxation Experiments under Fast MAS (60-110 kHz).How uniform is the peptide plane geometry? A high-accuracy NMR study of dipolar Cα-C'/H N-N cross-correlated relaxationSolid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain MotionNuclear Magnetic Resonance Methods for Studying Soluble, Fibrous, and Membrane-Embedded Proteins
P2860
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P2860
Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.
description
2008 nî lūn-bûn
@nan
2008 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մարտին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.
@ast
Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.
@en
type
label
Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.
@ast
Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.
@en
prefLabel
Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.
@ast
Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis.
@en
P2093
P356
P1476
Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis
@en
P2093
Dennis A Torchia
Lishan Yao
P304
P356
10.1021/JP0772124
P407
P50
P577
2008-03-22T00:00:00Z