(Q70170789)

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Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance

scientific article published on 01 October 1983

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scholarly article

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9 October 2019

Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance (English)

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9 October 2019

structural biology

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10.1016/S0022-2836(83)80144-2

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25 September 2023

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K Wüthrich

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9 October 2019

Martin Billeter

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9 October 2019

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W. Braun

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publication date

1 October 1983

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9 October 2019

5 October 1983

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25 September 2023

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25 September 2023

https://api.elsevier.com/content/article/PII:S0022283683801442?httpAccept=text/plain

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25 September 2023

Journal of Molecular Biology

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9 October 2019

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9 October 2019

949-961

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9 October 2019

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9 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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7 January 2021

Combined use of proton-proton overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagon

1 reference

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Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance

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High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface

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A simplified representation of protein conformations for rapid simulation of protein folding

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Computer simulation of protein folding

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Conformation of Polypeptides and Proteins

1 reference

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The interpretation of protein structures: Total volume, group volume distributions and packing density

1 reference

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7 January 2021

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

1 reference

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7 January 2021

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

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

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Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation

1

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10.1016/S0022-2836(83)80144-2

https://api.crossref.org/works/10.1016/S0022-2836(83)80144-2

25 September 2023

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10.1016/S0022-2836(83)80144-2

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Europe PubMed Central

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9 October 2019

1 reference

Europe PubMed Central

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9 October 2019

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