Investigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles.

The photochemically-induced dynamic nuclear polarization technique has been used to investigate the access of a photoexcited flavin dye to tyrosyl and histidyl residues in [Met]enkephalin and human and camel beta-endorphins, both alone and in the presence of n-dodecylphosphorylcholine micelles. The...

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Main Authors: Zetta, L, Hore, P, Kaptein, R
Format: Journal article
Language:English
Published: 1983
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author Zetta, L
Hore, P
Kaptein, R
author_facet Zetta, L
Hore, P
Kaptein, R
author_sort Zetta, L
collection OXFORD
description The photochemically-induced dynamic nuclear polarization technique has been used to investigate the access of a photoexcited flavin dye to tyrosyl and histidyl residues in [Met]enkephalin and human and camel beta-endorphins, both alone and in the presence of n-dodecylphosphorylcholine micelles. The results indicate that the mode of binding of Tyr-1, but not of residue 27, is similar in the two endorphins and differs from that of Tyr-1 in [Met]enkephalin. In human beta-endorphin, accessibility and mobility of Tyr-27 are strongly reduced in the presence of lipid at physiological pH, whereas in camel beta-endorphin His-27 becomes immobilized only at high pH. Moreover, nuclear Overhauser enhancement experiments suggest a rigidifying influence of the peptide on the polar head groups of the micelles.
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spelling oxford-uuid:c0e75c07-559d-4d85-b3e8-29ed7ae446672022-03-27T05:57:44ZInvestigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:c0e75c07-559d-4d85-b3e8-29ed7ae44667EnglishSymplectic Elements at Oxford1983Zetta, LHore, PKaptein, RThe photochemically-induced dynamic nuclear polarization technique has been used to investigate the access of a photoexcited flavin dye to tyrosyl and histidyl residues in [Met]enkephalin and human and camel beta-endorphins, both alone and in the presence of n-dodecylphosphorylcholine micelles. The results indicate that the mode of binding of Tyr-1, but not of residue 27, is similar in the two endorphins and differs from that of Tyr-1 in [Met]enkephalin. In human beta-endorphin, accessibility and mobility of Tyr-27 are strongly reduced in the presence of lipid at physiological pH, whereas in camel beta-endorphin His-27 becomes immobilized only at high pH. Moreover, nuclear Overhauser enhancement experiments suggest a rigidifying influence of the peptide on the polar head groups of the micelles.
spellingShingle Zetta, L
Hore, P
Kaptein, R
Investigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles.
title Investigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles.
title_full Investigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles.
title_fullStr Investigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles.
title_full_unstemmed Investigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles.
title_short Investigation by photochemically-induced dynamic nuclear polarization and nuclear Overhauser enhancement 1H-NMR of the interaction between beta-endorphin and phospholipid micelles.
title_sort investigation by photochemically induced dynamic nuclear polarization and nuclear overhauser enhancement 1h nmr of the interaction between beta endorphin and phospholipid micelles
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AT horep investigationbyphotochemicallyinduceddynamicnuclearpolarizationandnuclearoverhauserenhancement1hnmroftheinteractionbetweenbetaendorphinandphospholipidmicelles
AT kapteinr investigationbyphotochemicallyinduceddynamicnuclearpolarizationandnuclearoverhauserenhancement1hnmroftheinteractionbetweenbetaendorphinandphospholipidmicelles