(Q72684541)

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Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance

scientific article published on 01 September 1982

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28 October 2019

Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance (English)

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28 October 2019

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K Wüthrich

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28 October 2019

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G Wagner

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28 October 2019

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1 September 1982

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28 October 2019

Journal of Molecular Biology

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28 October 2019

160

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28 October 2019

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28 October 2019

343-361

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28 October 2019

Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations.

1 reference

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Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor

1 reference

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Two-dimensional spin echo correlated spectroscopy (SECSY) for 1H NMR studies of biological macromolecules

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Hydrogen exchange rates in pancreatic trypsin inhibitor are not correlated to thermal stability in urea

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Conformation and segmental motion of native and denatured ribonuclease A in solution. Application of natural-abundance carbon-13 partially relaxed Fourier transform nuclear magnetic resonance

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Mechanism of isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor

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Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance

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The internal dynamics of globular proteins.

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Carbon-13 nuclear magnetic resonance relaxation studies of internal mobility of the polypeptide chain in basic pancreatic trypsin inhibitor and a selectively reduced analog

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Studies of J-connectivities and selective 1H-1H Overhauser effects in H2O solutions of biological macromolecules by two-dimensional NMR experiments

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Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor

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Principles of protein-protein recognition

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Kinetics of the exchange of individual amide protons in the basic pancreatic trypsin inhibitor

1 reference

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Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI)

1 reference

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The anatomy and taxonomy of protein structure

1 reference

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The interpretation of protein structures: Estimation of static accessibility

1 reference

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p2H dependence of the exchange with the solvent of interior amide protons in basic pancreatic trypsin inhibitor modified by reduction of the disulfide bond 1438

1 reference

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Nuclear magnetic resonance measurement of hydrogen exchange kinetics of single protons in basic pancreatic trypsin inhibitor

1 reference

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Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 2. Combined use of correlated spectroscopy and nuclear Overhauser spectroscopy for sequential assignments of backbone resonances and elucidat

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Hydrogen Exchange in Proteins

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Hydrogen exchange

1 reference

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Structural interpretation of the amide proton exchange in the basic pancreatic trypsin inhibitor and related proteins

1 reference

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Assignment of the 1H nuclear magnetic resonance spectrum of the trypsin inhibitor E from Dendroaspis polylepis polylepis

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Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Glucagon bound to perdeuterated dodecylphosphocholine micelles.

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Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique.

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Correlations between internal mobility and stability of globular proteins

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Carboxypeptidase A: a protein and an enzyme.

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Two‐dimensional spectroscopy. Application to nuclear magnetic resonance

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Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at l.5 Å resolution

1 reference

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Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery

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Primary structure effects on peptide group hydrogen exchange.

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An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: Application to ribonuclease S peptide

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Nmr studies of aqueous solutions of tetra and branched peptides. I. Sequence determination of amino-acid residues and the assignment of peptide hydrogen signals

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Identifiers

10.1016/0022-2836(82)90180-2

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6184480%20AND%20SRC:MED&resulttype=core&format=json

28 October 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:6184480%20AND%20SRC:MED&resulttype=core&format=json

28 October 2019

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