NMR spectroscopy brings invisible protein states into focus. - Wikidata - wikimedia - TriplyDB

NMR spectroscopy brings invisible protein states into focus.

NMR spectroscopy brings invisible protein states into focus.

http://www.wikidata.org/entity/Q37617946

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A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis Mechanisms of amyloid formation revealed by solution NMR Seeing the invisible by paramagnetic and diamagnetic NMR Revealing the properties of plant defensins through dynamics Synergistic applications of MD and NMR for the study of biological systems The impact of a ligand binding on strand migration in the SAM-I riboswitch A transient and low-populated protein-folding intermediate at atomic resolution Regulation of the Plasmodium Motor Complex: PHOSPHORYLATION OF MYOSIN A TAIL-INTERACTING PROTEIN (MTIP) LOOSENS ITS GRIP ON MyoA Structure and dynamics of a primordial catalytic fold generated by in vitro evolution Analysing the visible conformational substates of the FK506-binding protein FKBP12 Structures of the Excited States of Phospholamban and Shifts in Their Populations upon Phosphorylation Spatial elucidation of motion in proteins by ensemble-based structure calculation using exact NOEs Incorporation of protein flexibility and conformational energy penalties in docking screens to improve ligand discovery Differential dynamic engagement within 24 SH3 domain: peptide complexes revealed by co-linear chemical shift perturbation analysis Probabilistic validation of protein NMR chemical shift assignments A simple model predicts experimental folding rates and a hub-like topology Determination of pseudocontact shifts of low-populated excited states by NMR chemical exchange saturation transfer.Multi-timescale conformational dynamics of the SH3 domain of CD2-associated protein using NMR spectroscopy and accelerated molecular dynamics pH-dependent transient conformational states control optical properties in cyan fluorescent protein NMR approaches in structure-based lead discovery: recent developments and new frontiers for targeting multi-protein complexes Integrating atomistic molecular dynamics simulations, experiments, and network analysis to study protein dynamics: strength in unity.Structure-Based Assignment of Ile, Leu, and Val Methyl Groups in the Active and Inactive Forms of the Mitogen-Activated Protein Kinase Extracellular Signal-Regulated Kinase 2 A New Method for Determining Structure Ensemble: Application to a RNA Binding Di-Domain Protein.Predicting Real-Valued Protein Residue Fluctuation Using FlexPred.Alternate states of proteins revealed by detailed energy landscape mapping Recent excitements in protein NMR: Large proteins and biologically relevant dynamics.Protein folding at single-molecule resolution.Advances in automated NMR protein structure determination.An optimal distance cutoff for contact-based Protein Structure Networks using side-chain centers of mass.Structural features that predict real-value fluctuations of globular proteins Protein activity regulation by conformational entropy.Pathway and mechanism of drug binding to G-protein-coupled receptors.Investigating the mechanisms of amylolysis of starch granules by solution-state NMR.Defining a length scale for millisecond-timescale protein conformational exchange.Recovering a representative conformational ensemble from underdetermined macromolecular structural data.Banding of NMR-derived methyl order parameters: implications for protein dynamics.The alteration of the C-terminal region of human frataxin distorts its structural dynamics and function.Development of a method for reconstruction of crowded NMR spectra from undersampled time-domain data Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.Biophysical characterization of recombinant proteins: a key to higher structural genomics success

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P2860

NMR spectroscopy brings invisible protein states into focus.

http://www.wikidata.org/entity/Q37617946

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年學術文章

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2009年學術文章

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2009年學術文章

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name

NMR spectroscopy brings invisible protein states into focus.

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NMR spectroscopy brings invisible protein states into focus.

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type

label

NMR spectroscopy brings invisible protein states into focus.

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NMR spectroscopy brings invisible protein states into focus.

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NMR spectroscopy brings invisible protein states into focus.

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NMR spectroscopy brings invisible protein states into focus.

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Nature Chemical Biology

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NMR spectroscopy brings invisible protein states into focus.

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Andrew J Baldwin

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P2860

Relaxation Processes in a System of Two Spins

Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy

A consensus view of protein dynamics

Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance Experiments

Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR

Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution

Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein folding

Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy

Multiple conformational changes in enzyme catalysis

Dynamical contributions to enzyme catalysis: critical tests of a popular hypothesis

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10.1038/NCHEMBIO.238

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19841630

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