Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra.
The hydrogen exchange behavior of exchangeable protons in proteins can provide important information for understanding the principles of protein structure and function. The positions and exchange rates of the slowly-exchanging amide protons in sperm whale myoglobin have been mapped using 15N-1H NMR...
Main Authors: | , , , , |
---|---|
Format: | Text |
Language: | English |
Published: |
Cold Spring Harbor Laboratory Press
2000
|
Subjects: | |
Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144433 http://www.ncbi.nlm.nih.gov/pubmed/10739261 |
id |
ftpubmed:oai:pubmedcentral.nih.gov:2144433 |
---|---|
record_format |
openpolar |
spelling |
ftpubmed:oai:pubmedcentral.nih.gov:2144433 2023-05-15T18:26:36+02:00 Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra. Cavagnero, S. Thériault, Y. Narula, S. S. Dyson, H. J. Wright, P. E. 2000-01 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144433 http://www.ncbi.nlm.nih.gov/pubmed/10739261 en eng Cold Spring Harbor Laboratory Press http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144433 http://www.ncbi.nlm.nih.gov/pubmed/10739261 Research Article Text 2000 ftpubmed 2013-09-01T10:31:29Z The hydrogen exchange behavior of exchangeable protons in proteins can provide important information for understanding the principles of protein structure and function. The positions and exchange rates of the slowly-exchanging amide protons in sperm whale myoglobin have been mapped using 15N-1H NMR spectroscopy. The slowest-exchanging amide protons are those that are hydrogen bonded in the longest helices, including members of the B, E, and H helices. Significant protection factors were observed also in the A, C, and G helices, and for a few residues in the D and F helices. Knowledge of the identity of slowly-exchanging amide protons forms the basis for the extensive quench-flow kinetic folding experiments that have been performed for myoglobin, and gives insights into the tertiary interactions and dynamics in the protein. Text Sperm whale PubMed Central (PMC) |
institution |
Open Polar |
collection |
PubMed Central (PMC) |
op_collection_id |
ftpubmed |
language |
English |
topic |
Research Article |
spellingShingle |
Research Article Cavagnero, S. Thériault, Y. Narula, S. S. Dyson, H. J. Wright, P. E. Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra. |
topic_facet |
Research Article |
description |
The hydrogen exchange behavior of exchangeable protons in proteins can provide important information for understanding the principles of protein structure and function. The positions and exchange rates of the slowly-exchanging amide protons in sperm whale myoglobin have been mapped using 15N-1H NMR spectroscopy. The slowest-exchanging amide protons are those that are hydrogen bonded in the longest helices, including members of the B, E, and H helices. Significant protection factors were observed also in the A, C, and G helices, and for a few residues in the D and F helices. Knowledge of the identity of slowly-exchanging amide protons forms the basis for the extensive quench-flow kinetic folding experiments that have been performed for myoglobin, and gives insights into the tertiary interactions and dynamics in the protein. |
format |
Text |
author |
Cavagnero, S. Thériault, Y. Narula, S. S. Dyson, H. J. Wright, P. E. |
author_facet |
Cavagnero, S. Thériault, Y. Narula, S. S. Dyson, H. J. Wright, P. E. |
author_sort |
Cavagnero, S. |
title |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra. |
title_short |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra. |
title_full |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra. |
title_fullStr |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra. |
title_full_unstemmed |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15N-1H NMR spectra. |
title_sort |
amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15n-1h nmr spectra. |
publisher |
Cold Spring Harbor Laboratory Press |
publishDate |
2000 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144433 http://www.ncbi.nlm.nih.gov/pubmed/10739261 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144433 http://www.ncbi.nlm.nih.gov/pubmed/10739261 |
_version_ |
1766208572831563776 |