Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
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Hepcidin revisited, disulfide connectivity, dynamics, and structureThe solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated proteinSolution structure of Compstatin, a potent complement inhibitorLocal order in the unfolded state: conformational biases and nearest neighbor interactionsStructure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's diseaseCharacterization and NMR solution structure of a novel cyclic pentapeptide inhibitor of pathogenic hantavirusesElongation of the BH8 beta-hairpin peptide: Electrostatic interactions in beta-hairpin formation and stabilityGrand challenges in cellular biochemistry: the "next-gen" biochemistryToward direct determination of conformations of protein building units from multidimensional NMR experiments. V. NMR chemical shielding analysis of N-formyl-serinamide, a model for polar side-chain containing peptides.High accuracy of Karplus equations for relating three-bond J couplings to protein backbone torsion angles.Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues.A protocol for the refinement of NMR structures using simultaneously pseudocontact shift restraints from multiple lanthanide ions.Overview on the use of NMR to examine protein structure.Distance geometry and related methods for protein structure determination from NMR data.On the calculation of ³Jαβ-coupling constants for side chains in proteins.Rapid calculation of protein chemical shifts using bond polarization theory and its application to protein structure refinement.NMR analysis of human salivary mucin (MUC7) derived O-linked model glycopeptides: comparison of structural features and carbohydrate-peptide interactions.Structural heterogeneity in familial Alzheimer's disease mutants of amyloid-beta peptides.Two new bicyclic cembranolides from a new Sarcophyton species and determination of the absolute configuration of sarcoglaucol-16-one.The polyproline II conformation in short alanine peptides is noncooperativeIntrinsic backbone preferences are fully present in blocked amino acidsOrigin of the neighboring residue effect on peptide backbone conformation.Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: distributions of phi.Study of spontaneous E/Z isomerization of bis[(Z)-cyanomethylidene]-diazapentacyclodienedicarboxylates by 1 H, 13 C, and 15 N NMR spectroscopy, X-ray, and quantum chemical calculation data.Deriving Structural Information from Experimentally Measured Data on Biomolecules.Spectral data of two new asymmetric sesquiterpene alcohols: (14R)-beta-oplopenol and (14S)-beta-oplopenol.The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins.Polyproline II structure in a sequence of seven alanine residues.Helical content of a β(3)-octapeptide in methanol: molecular dynamics simulations explain a seeming discrepancy between conclusions derived from CD and NMR data.A comprehensive library of blocked dipeptides reveals intrinsic backbone conformational propensities of unfolded proteins.An improved structural characterisation of reduced French bean plastocyanin based on NMR data and local-elevation molecular dynamics simulation.Conformations of islet amyloid polypeptide monomers in a membrane environment: implications for fibril formation.Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins.The intrinsic conformational features of amino acids from a protein coil library and their applications in force field development.Relativistic effects in the one-bond spin-spin coupling constants involving selenium.Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolutionForce field-dependent solution properties of glycine oligomersIs the Conformational Ensemble of Alzheimer's Aβ10-40 Peptide Force Field Dependent?Assessing and refining molecular dynamics simulations of proteins with nuclear magnetic resonance data.Promiscuous contacts and heightened dynamics increase thermostability in an engineered variant of the engrailed homeodomain
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P2860
Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
description
im Januar 1959 veröffentlichter wissenschaftlicher Artikel
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wetenschappelijk artikel
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наукова стаття, опублікована в січні 1959
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Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
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Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
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Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
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Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
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Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
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Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
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P356
P1476
Contact Electron‐Spin Coupling of Nuclear Magnetic Moments
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P356
10.1063/1.1729860
P407
P577
1959-01-01T00:00:00Z