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Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles

scientific article published on January 1987

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Europe PubMed Central

18 October 2017

Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles (English)

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Europe PubMed Central

18 October 2017

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3

K Wüthrich

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Europe PubMed Central

18 October 2017

K H Lee

1

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Europe PubMed Central

PubMed ID

3801489

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18 October 2017

J E Fitton

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2

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Europe PubMed Central

18 October 2017

1 January 1987

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Europe PubMed Central

18 October 2017

Biochimica et Biophysica Acta

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Europe PubMed Central

18 October 2017

911

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Europe PubMed Central

18 October 2017

2

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Europe PubMed Central

18 October 2017

144-153

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Europe PubMed Central

18 October 2017

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

1 reference

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

1 reference

9 October 2022

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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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The amino acid sequence of the delta haemolysin of Staphylococcus aureus

1 reference

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Sensitive assay for detection of toxin-induced damage to the cytoplasmic membrane of human diploid fibroblasts

1 reference

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Physicochemical characterization of glucagon-containing lipid micelles

1 reference

9 October 2022

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Systematic application of high-resolution, phase-sensitive two-dimensional 1H-NMR techniques for the identification of the amino-acid-proton spin systems in proteins. Rabbit metallothionein-2

1 reference

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Two‐dimensional spectroscopy. Application to nuclear magnetic resonance

1 reference

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Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances

1 reference

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Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins

1 reference

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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

1 reference

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The hemolysins of Staphylococcus aureus

1 reference

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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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Use of fully deuterated micelles for conformational studies of membrane proteins by high resolution 1H nuclear magnetic resonance

1 reference

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Physicochemical studies of the protein-lipid interactions in melittin-containing micelles

1 reference

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Location and orientation relative to the micelle surface for glucagon in mixed micelles with dodecylphosphocholine EPR and NMR studies

1 reference

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Lytic effects of melittin and delta-haemolysin from Staphylococcus aureus on vesicles of dipalmitoylphosphatidylcholine

1 reference

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Determination of toxin-induced leakage of different-size nucleotides through the plasma membrane of human diploid fibroblasts

1 reference

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High-resolution 1H-NMR studies of self-aggregation of melittin in aqueous solution

1 reference

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

1 reference

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Physicochemical studies on delta haemolysin, a staphylococcal cytolytic polypeptide

1 reference

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Melittin bound to dodecylphosphocholine micelles 1H-NMR assignments and global conformational features

1 reference

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10.1016/0167-4838(87)90003-3

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Europe PubMed Central

18 October 2017

release_abmpbmel5fhapiammhbxa3xra4

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PubMed ID

3801489

1 reference

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Europe PubMed Central

PubMed ID

3801489

retrieved

18 October 2017

(Q42223425)

Nuclear magnetic resonance investigation of the conformation of delta-haemolysin bound to dodecylphosphocholine micelles

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