Proton Nuclear Magnetic Resonance Studies of Myoglobin in H2O
Exchangeable hydrogens in proteins can be identified by comparison of nuclear magnetic resonance spectra obtained in H2O and in D2O. In oxymyoglobin and myoglobin we have been able to observe resonances of the NH protons of the two tryptophans, as well as one resonance from arginine and one from his...
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ftpubmed:oai:pubmedcentral.nih.gov:283324 2023-05-15T18:26:41+02:00 Proton Nuclear Magnetic Resonance Studies of Myoglobin in H2O Patel, Dinshaw J. Kampa, L. Shulman, R. G. Yamane, T. Wyluda, B. J. 1970-11 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC283324 http://www.ncbi.nlm.nih.gov/pubmed/5274441 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC283324 http://www.ncbi.nlm.nih.gov/pubmed/5274441 Physical Sciences: Chemistry Text 1970 ftpubmed 2013-08-29T17:55:49Z Exchangeable hydrogens in proteins can be identified by comparison of nuclear magnetic resonance spectra obtained in H2O and in D2O. In oxymyoglobin and myoglobin we have been able to observe resonances of the NH protons of the two tryptophans, as well as one resonance from arginine and one from histidine in the range -10 to -15 ppm downfield from 3-(trimethylsilyl)propanesulfonic acid (sodium salt). These resonances have been identified by chemical modifications coupled with considerations of crystallographic structure and the dependence of the resonances on the species (sperm whale, porpoise, horse) from which the myglobin was obtained and on spin, pH, and temperature. Text Sperm whale PubMed Central (PMC) |
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Physical Sciences: Chemistry |
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Physical Sciences: Chemistry Patel, Dinshaw J. Kampa, L. Shulman, R. G. Yamane, T. Wyluda, B. J. Proton Nuclear Magnetic Resonance Studies of Myoglobin in H2O |
topic_facet |
Physical Sciences: Chemistry |
description |
Exchangeable hydrogens in proteins can be identified by comparison of nuclear magnetic resonance spectra obtained in H2O and in D2O. In oxymyoglobin and myoglobin we have been able to observe resonances of the NH protons of the two tryptophans, as well as one resonance from arginine and one from histidine in the range -10 to -15 ppm downfield from 3-(trimethylsilyl)propanesulfonic acid (sodium salt). These resonances have been identified by chemical modifications coupled with considerations of crystallographic structure and the dependence of the resonances on the species (sperm whale, porpoise, horse) from which the myglobin was obtained and on spin, pH, and temperature. |
format |
Text |
author |
Patel, Dinshaw J. Kampa, L. Shulman, R. G. Yamane, T. Wyluda, B. J. |
author_facet |
Patel, Dinshaw J. Kampa, L. Shulman, R. G. Yamane, T. Wyluda, B. J. |
author_sort |
Patel, Dinshaw J. |
title |
Proton Nuclear Magnetic Resonance Studies of Myoglobin in H2O |
title_short |
Proton Nuclear Magnetic Resonance Studies of Myoglobin in H2O |
title_full |
Proton Nuclear Magnetic Resonance Studies of Myoglobin in H2O |
title_fullStr |
Proton Nuclear Magnetic Resonance Studies of Myoglobin in H2O |
title_full_unstemmed |
Proton Nuclear Magnetic Resonance Studies of Myoglobin in H2O |
title_sort |
proton nuclear magnetic resonance studies of myoglobin in h2o |
publishDate |
1970 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC283324 http://www.ncbi.nlm.nih.gov/pubmed/5274441 |
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Sperm whale |
genre_facet |
Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC283324 http://www.ncbi.nlm.nih.gov/pubmed/5274441 |
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1766208652334596096 |