Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
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The Human W42R D-Crystallin Mutant Structure Provides a Link between Congenital and Age-related CataractsHYDROGEN BOND AND INTERNAL SOLVENT DYNAMICS OF BPTI PROTEINSequence specific 1H-NMR assignments and secondary structure of a carboxy-terminal functional fragment of apolipoprotein CIIAbeta amyloid fibrils possess a core structure highly resistant to hydrogen exchangeConformational dynamics of insulin.Solution phase conformation and proteolytic stability of amide-linked neuraminic acid analogues.Interaction of the water-soluble protein aprotinin with liposomes: gel-filtration, turbidity studies, and 31P NMR studies.Proton-proton Overhauser NMR spectroscopy with polypeptide chains in large structures.Effect of glycerol on the interactions and solubility of bovine pancreatic trypsin inhibitorCorrelations between internal mobility and stability of globular proteins.Hydrogen isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitorMillisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature.Genetic assignment of resonances in the NMR spectrum of a protein: lac repressor.Spider wrapping silk fibre architecture arising from its modular soluble protein precursor.Speeding up direct (15)N detection: hCaN 2D NMR experiment.Protein-Inhibitor Interaction Studies Using NMRAsymmetric protonation of EmrE.Enhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrilsConformational Selection and Induced Fit Mechanisms in the Binding of an Anticancer Drug to the c-Src KinaseProgress in ab initio QM/MM free-energy simulations of electrostatic energies in proteins: accelerated QM/MM studies of pKa, redox reactions and solvation free energiesGetting the chemistry right: protonation, tautomers and the importance of H atoms in biological chemistry.Magnetic resonance characterization of ischemic tissue metabolism.Protein self-association in solution: the bovine pancreatic trypsin inhibitor decamer.Folding analysis of hormonal polypeptide calcitonins and the oxidized calcitonins using electrospray ionization mass spectrometry combined with H/D exchange.On the pH dependence of amide proton exchange rates in proteins.ESI hydrogen/deuterium exchange can count chemical forms of heteroatom-bound hydrogen.pH-dependent random coil (1)H, (13)C, and (15)N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements.Internal packing conditions and fluctuations of amino acid residues in globular proteins.Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences.Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes.Implications of a high dielectric constant in proteins1H-NMR sequential assignments and cation-binding studies of spinach plastocyanin
P2860
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P2860
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
description
1979 nî lūn-bûn
@nan
1979年の論文
@ja
1979年学术文章
@wuu
1979年学术文章
@zh-cn
1979年学术文章
@zh-hans
1979年学术文章
@zh-my
1979年学术文章
@zh-sg
1979年學術文章
@yue
1979年學術文章
@zh
1979年學術文章
@zh-hant
name
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
@en
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
@nl
type
label
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
@en
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
@nl
prefLabel
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
@en
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
@nl
P1476
Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor.
@en
P2093
P356
10.1016/0022-2836(79)90548-5
P407
P577
1979-05-01T00:00:00Z