Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance (Q72684541)

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scientific article published on 01 September 1982

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English	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

publication date

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.

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

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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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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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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

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

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The anatomy and taxonomy of protein structure

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The interpretation of protein structures: Estimation of static accessibility

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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

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

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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

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

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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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