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

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Conformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/S0022-2836(83)80143-0
P3181OpenCitations bibliographic resource ID3228952
P698PubMed publication ID6631957
P5875ResearchGate publication ID16564287

P50authorKurt WüthrichQ110957
Gerhard WiderQ56396398
P2093author name stringK H Lee
W Braun
P2860cites workSequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonanceQ57825975
Two-dimensional spin echo correlated spectroscopy (SECSY) for 1H NMR studies of biological macromoleculesQ66955030
Use of fully deuterated micelles for conformational studies of membrane proteins by high resolution 1H nuclear magnetic resonanceQ67005386
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 resonanceQ70170789
Proton NMR studies of the association and folding of glucagon in solutionQ71359926
Studies on the Conformation of GlucagonQ71761339
Conformational states of glucagonQ72326204
The circular dichroism of glucagon solutionsQ72358938
Conformational studies of lipid-bound polypeptides by elucidation of proton-proton cross-relaxation networksQ72864525
Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine EPR and NMR studiesQ72908108
X-ray analysis of glucagon and its relationship to receptor bindingQ27643265
Gene duplications in the structural evolution of chymotrypsinQ28239251
The anatomy and taxonomy of protein structureQ28277011
High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interfaceQ28366140
A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromoleculesQ29616473
Conformation of Polypeptides and ProteinsQ29617878
Conformational nature of monomeric glucagonQ36532972
Studies of J-connectivities and selective 1H-1H Overhauser effects in H2O solutions of biological macromolecules by two-dimensional NMR experimentsQ36589342
Conformational transitions of glucagon in solution: The α → β transitionQ39163582
The Conformation, Flexibility, and Dynamics of Polypeptide HormonesQ40087818
The internal dynamics of globular proteins.Q40300077
Glucagon-sensitive adenyl cylase in plasma membrane of hepatic parenchymal cellsQ42231721
Combined use of proton-proton overhauser enhancements and a distance geometry algorithm for determination of polypeptide conformations. Application to micelle-bound glucagonQ42244998
Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Glucagon bound to perdeuterated dodecylphosphocholine micelles.Q42263758
Physicochemical characterization of glucagon-containing lipid micellesQ42273941
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.Q51660150
Interaction of glucagon with dimyristoyl glycerophosphocholine.Q53731017
P433issue4
P407language of work or nameEnglishQ1860
P921main subjectglucagonQ28163629
P304page(s)921-48
P577publication date1983-10-05
P1433published inJournal of Molecular BiologyQ925779
P1476titleConformation of glucagon in a lipid-water interphase by 1H nuclear magnetic resonance
P478volume169

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