Cargando…

Conformational exchange of aromatic side chains characterized by L-optimized TROSY-selected (13)C CPMG relaxation dispersion

Protein dynamics on the millisecond time scale commonly reflect conformational transitions between distinct functional states. NMR relaxation dispersion experiments have provided important insights into biologically relevant dynamics with site-specific resolution, primarily targeting the protein bac...

Descripción completa

Detalles Bibliográficos
Autores principales:	Weininger, Ulrich, Respondek, Michal, Akke, Mikael
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Springer Netherlands 2012
Materias:	Communication
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3427480/ https://www.ncbi.nlm.nih.gov/pubmed/22833056 http://dx.doi.org/10.1007/s10858-012-9656-z

Ejemplares similares

Conformational exchange of aromatic side chains by (1)H CPMG relaxation dispersion
por: Raum, Heiner N., et al.
Publicado: (2018)

Off-resonance rotating-frame relaxation dispersion experiment for (13)C in aromatic side chains using L-optimized TROSY-selection
por: Weininger, Ulrich, et al.
Publicado: (2014)

(13)C relaxation experiments for aromatic side chains employing longitudinal- and transverse-relaxation optimized NMR spectroscopy
por: Weininger, Ulrich, et al.
Publicado: (2012)

(1)H R(1ρ) relaxation dispersion experiments in aromatic side chains
por: Dreydoppel, Matthias, et al.
Publicado: (2021)

Site-selective (1)H/(2)H labeling enables artifact-free (1)H CPMG relaxation dispersion experiments in aromatic side chains
por: Raum, Heiner N., et al.
Publicado: (2019)

Characterizing Fast Conformational Exchange of Aromatic Rings Using Residual Dipolar Couplings: Distinguishing Jumplike Flips from Other Exchange Mechanisms
por: Dreydoppel, Matthias, et al.
Publicado: (2022)

NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins
por: Akke, Mikael, et al.
Publicado: (2023)

Analysis of conformational exchange processes using methyl-TROSY-based Hahn echo measurements of quadruple-quantum relaxation
por: Waudby, Christopher A., et al.
Publicado: (2021)

Slow ring flips in aromatic cluster of GB1 studied by aromatic (13)C relaxation dispersion methods
por: Dreydoppel, Matthias, et al.
Publicado: (2020)

Probing RNA dynamics via longitudinal exchange and CPMG relaxation dispersion NMR spectroscopy using a sensitive (13)C-methyl label
por: Kloiber, Karin, et al.
Publicado: (2011)

Specific (12)C(β)D(2)(12)C(γ)D(2)S(13)C(ε)HD(2) Isotopomer Labeling of Methionine To Characterize Protein Dynamics by (1)H and (13)C NMR Relaxation Dispersion
por: Weininger, Ulrich, et al.
Publicado: (2012)

Aromatic (19)F–(13)C TROSY—[(19)F, (13)C]‐Pyrimidine Labeling for NMR Spectroscopy of RNA
por: Nußbaumer, Felix, et al.
Publicado: (2020)

Aromatic (19)F-(13)C TROSY: A background-free approach to probe biomolecular structure, function and dynamics
por: Boeszoermenyi, Andras, et al.
Publicado: (2019)

Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations
por: Dreydoppel, Matthias, et al.
Publicado: (2021)

An exact solution for R(2,)(eff) in CPMG experiments in the case of two site chemical exchange
por: Baldwin, Andrew J.
Publicado: (2014)

Microstructural Analysis of Peripheral Lung Tissue through CPMG Inter-Echo Time R2 Dispersion
por: Kurz, Felix T., et al.
Publicado: (2015)

Pure shift amide detection in conventional and TROSY-type experiments of (13)C,(15)N-labeled proteins
por: Haller, Jens D., et al.
Publicado: (2022)

Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination
por: Diarra dit Konté, Nana, et al.
Publicado: (2017)

Ultrastructural evidence for self-replication of Alzheimer-associated Aβ42 amyloid along the sides of fibrils
por: Törnquist, Mattias, et al.
Publicado: (2020)

Aromatic side-chain flips orchestrate the conformational sampling of functional loops in human histone deacetylase 8
por: Shukla, Vaibhav Kumar, et al.
Publicado: (2021)

Mapping the energy landscape of protein–ligand binding via linear free energy relationships determined by protein NMR relaxation dispersion
por: Stenström, Olof, et al.
Publicado: (2020)

Observation of Arginine Side-Chain Motions Coupled to the Global Conformational Exchange Process in Deubiquitinase A
por: Kabra, Ashish, et al.
Publicado: (2022)

On Side-Chain Conformational Entropy of Proteins
por: Zhang, Jinfeng, et al.
Publicado: (2006)

Biphasic activation of β-arrestin 1 upon interaction with a GPCR revealed by methyl-TROSY NMR
por: Shiraishi, Yutaro, et al.
Publicado: (2021)

Stability and sensitivity of water T (2) obtained with IDEAL‐CPMG in healthy and fat‐infiltrated skeletal muscle
por: Sinclair, Christopher D.J., et al.
Publicado: (2016)

Quantitative T(2) Mapping of Knee Cartilage: Comparison between the Synthetic MR Imaging and the CPMG Sequence
por: Lee, Seung Hyun, et al.
Publicado: (2018)

Arginine Side‐Chain Hydrogen Exchange: Quantifying Arginine Side‐Chain Interactions in Solution
por: Mackenzie, Harold W., et al.
Publicado: (2018)

Side-Chain Length and Dispersity in ROMP Polymers with Pore-Generating Side Chains for Gas Separations
por: Benedetti, Francesco M., et al.
Publicado: (2022)

Minute Additions of DMSO Affect Protein Dynamics Measurements by NMR Relaxation Experiments through Significant Changes in Solvent Viscosity
por: Wallerstein, Johan, et al.
Publicado: (2018)

Fast and accurate prediction of protein side-chain conformations
por: Liang, Shide, et al.
Publicado: (2011)

Side Chain Conformational Averaging in Human Dihydrofolate Reductase
por: Tuttle, Lisa M., et al.
Publicado: (2014)

Quantifying side-chain conformational variations in protein structure
por: Miao, Zhichao, et al.
Publicado: (2016)

Influence of Side Chain Conformation on the Activity of Glycosidase Inhibitors
por: Tseng, Po‐Sen, et al.
Publicado: (2023)

Site-selective (13)C labeling of proteins using erythrose
por: Weininger, Ulrich
Publicado: (2017)

Selenoglycosides as Lectin Ligands: (77)Se‐Edited CPMG‐HSQMBC NMR Spectroscopy To Monitor Biomedically Relevant Interactions
por: Raics, Mária, et al.
Publicado: (2019)

Reconstructing Reliable Powder Patterns from Spikelets (Q)CPMG NMR Spectra: Simplification of UWNMR Crystallography Analysis
por: Mahun, Andrii, et al.
Publicado: (2021)

Site-selective (13)C labeling of histidine and tryptophan using ribose
por: Weininger, Ulrich
Publicado: (2017)

Quantifying Microsecond Exchange in Large Protein Complexes with Accelerated Relaxation Dispersion Experiments in the Solid State
por: Öster, Carl, et al.
Publicado: (2019)

Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
por: Quistgaard, Esben M., et al.
Publicado: (2016)

Ligand binding remodels protein side-chain conformational heterogeneity
por: Wankowicz, Stephanie A, et al.
Publicado: (2022)

Cannot write session to /tmp/vufind_sessions/sess_u1hg6o5vta5ou2il98hrk5lij0