New tools provide new insights in NMR studies of protein dynamics.
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A dynamic knockout reveals that conformational fluctuations influence the chemical step of enzyme catalysisEfficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complexProtein folding: then and nowCryo-EM studies of the structure and dynamics of vacuolar-type ATPasesNMR Methods to Study Dynamic AllosteryInsights into Protein-Ligand Interactions: Mechanisms, Models, and MethodsUV resonance Raman investigations of peptide and protein structure and dynamicsConformational selection in protein binding and functionTowards physiological complexity with in vitro single-molecule biophysicsExploring the role of receptor flexibility in structure-based drug discoveryBridging between NMA and Elastic Network Models: Preserving All-Atom Accuracy in Coarse-Grained ModelsModeling conformational ensembles of slow functional motions in Pin1-WWDetection of functional modes in protein dynamicsConformational instability of the MARK3 UBA domain compromises ubiquitin recognition and promotes interaction with the adjacent kinase domainInterconversion between two unrelated protein folds in the lymphotactin native stateRecognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solutionHeterogeneity and dynamics in villin headpiece crystal structuresHidden alternative structures of proline isomerase essential for catalysisCrystallographic and Nuclear Magnetic Resonance Evaluation of the Impact of Peptide Binding to the Second PDZ Domain of Protein Tyrosine Phosphatase 1EAppropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinEStructural basis for regulation of the Crk signaling protein by a proline switch.Structures of domains I and IV from YbbR are representative of a widely distributed protein familyNMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin α1β1Accessing protein conformational ensembles using room-temperature X-ray crystallographyStructure and Dynamics of the Second CARD of Human RIG-I Provide Mechanistic Insights into Regulation of RIG-I ActivationStructural Instability Tuning as a Regulatory Mechanism in Protein-Protein InteractionsAllosteric Communication in the KIX Domain Proceeds through Dynamic Repacking of the Hydrophobic CoreStructure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMRDetermination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplingsStructural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneStructural determinants of ligand binding in the ternary complex of human ileal bile acid binding protein with glycocholate and glycochenodeoxycholate obtained from solution NMRWhen fast is better: protein folding fundamentals and mechanisms from ultrafast approachesKeep on moving: discovering and perturbing the conformational dynamics of enzymesNanoscale protein dynamics: a new frontier for neutron spin echo spectroscopyVPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteinsAlternative ground states enable pathway switching in biological electron transferCorrelating Calmodulin Landscapes with Chemical Catalysis in Neuronal Nitric Oxide Synthase using Time-Resolved FRET and a 5-Deazaflavin Thermodynamic TrapFold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergenAtomic-level characterization of the structural dynamics of proteinsThe role of dynamic conformational ensembles in biomolecular recognition
P2860
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P2860
New tools provide new insights in NMR studies of protein dynamics.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
New tools provide new insights in NMR studies of protein dynamics.
@ast
New tools provide new insights in NMR studies of protein dynamics.
@en
type
label
New tools provide new insights in NMR studies of protein dynamics.
@ast
New tools provide new insights in NMR studies of protein dynamics.
@en
prefLabel
New tools provide new insights in NMR studies of protein dynamics.
@ast
New tools provide new insights in NMR studies of protein dynamics.
@en
P356
P1433
P1476
New tools provide new insights in NMR studies of protein dynamics.
@en
P2093
Anthony Mittermaier
P304
P356
10.1126/SCIENCE.1124964
P407
P50
P577
2006-04-01T00:00:00Z