Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance (Q57825975)

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scientific article published on 01 March 1982

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English	Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance	scientific article published on 01 March 1982

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scholarly article

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10 October 2019

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

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10 October 2019

protein structure

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2

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10 October 2019

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K Wüthrich

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10 October 2019

author name string

G Wagner

3

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10 October 2019

W Braun

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publication date

1 March 1982

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10 October 2019

Journal of Molecular Biology

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10 October 2019

155

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10 October 2019

3

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10 October 2019

311-319

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10 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

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Individual assignments of amide proton resonances in the proton NMR spectrum of the basic pancreatic trypsin inhibitor

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Distance constraints on macromolecular conformation

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A Study of the Lysyl Residues in the Basic Pancreatic Trypsin Inhibitor using 1H Nuclear Magnetic Resonance at 360 MHz

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

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The anatomy and taxonomy of protein structure

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Systematic application of two-dimensional 1H nuclear-magnetic-resonance techniques for studies of proteins. 1. Combined use of spin-echo-correlated spectroscopy and J-resolved spectroscopy for the identification of complete spin systems of non-labil

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

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A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

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The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor. 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor

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Identifiers

10.1016/0022-2836(82)90007-9

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7077675%20AND%20SRC:MED&resulttype=core&format=json

10 October 2019

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7077675%20AND%20SRC:MED&resulttype=core&format=json

10 October 2019

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