Conformational distributions of unfolded polypeptides from novel NMR techniques
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MetaDisorder: a meta-server for the prediction of intrinsic disorder in proteinsUnfolded-state dynamics and structure of protein L characterized by simulation and experimentCorrelated inter-domain motions in adenylate kinaseBiophysical properties of intrinsically disordered p130Cas substrate domain--implication in mechanosensingAverage conformations determined from PRE data provide high-resolution maps of transient tertiary interactions in disordered proteins.Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance.Intrinsically disordered regions may lower the hydration free energy in proteins: a case study of nudix hydrolase in the bacterium Deinococcus radiodurans.Structural heterogeneity in the intrinsically disordered RNA polymerase II C-terminal domain.Expanding the proteome: disordered and alternatively folded proteins.A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein.Paramagnetic-based NMR restraints lift residual dipolar coupling degeneracy in multidomain detergent-solubilized membrane proteins.Just a Flexible Linker? The Structural and Dynamic Properties of CBP-ID4 Revealed by NMR Spectroscopy.Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structureConstructing RNA dynamical ensembles by combining MD and motionally decoupled NMR RDCs: new insights into RNA dynamics and adaptive ligand recognition.Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS.A self-consistent description of the conformational behavior of chemically denatured proteins from NMR and small angle scattering.Finding order within disorder: elucidating the structure of proteins associated with neurodegenerative disease.Towards a robust description of intrinsic protein disorder using nuclear magnetic resonance spectroscopy.How random are intrinsically disordered proteins? A small angle scattering perspective.Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins.Conformational propensities of intrinsically disordered proteins from NMR chemical shifts.Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods.Relative importance of first and second derivatives of nuclear magnetic resonance chemical shifts and spin-spin coupling constants for vibrational averaging.Structure and Dynamics of Ribosomal Protein L12: An Ensemble Model Based on SAXS and NMR Relaxation.Sequence determinants of compaction in intrinsically disordered proteins.Probing the urea dependence of residual structure in denatured human alpha-lactalbumin.Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations.Direct prediction of NMR residual dipolar couplings from the primary sequence of unfolded proteins.VirtualSpectrum, a tool for simulating peak list for multi-dimensional NMR spectra.Structural characterization by NMR of a double phosphorylated chimeric peptide vaccine for treatment of Alzheimer's disease.Application of long-range order to predict unfolding rates of two-state proteins.Idiosyncrasies of hnRNP A1-RNA recognition: Can binding mode influence function.Measurement of Structural Restraints
P2860
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P2860
Conformational distributions of unfolded polypeptides from novel NMR techniques
description
im Februar 2008 veröffentlichter wissenschaftlicher Artikel
@de
wetenschappelijk artikel
@nl
наукова стаття, опублікована в лютому 2008
@uk
name
Conformational distributions of unfolded polypeptides from novel NMR techniques
@en
Conformational distributions of unfolded polypeptides from novel NMR techniques
@nl
type
label
Conformational distributions of unfolded polypeptides from novel NMR techniques
@en
Conformational distributions of unfolded polypeptides from novel NMR techniques
@nl
prefLabel
Conformational distributions of unfolded polypeptides from novel NMR techniques
@en
Conformational distributions of unfolded polypeptides from novel NMR techniques
@nl
P2860
P356
P1476
Conformational distributions of unfolded polypeptides from novel NMR techniques
@en
P2093
Martin Blackledge
P2860
P304
P356
10.1063/1.2838167
P407
P577
2008-02-07T00:00:00Z