Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 N‐ 1 H NMR spectra
Abstract 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 15...
Published in: | Protein Science |
---|---|
Main Authors: | , , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2000
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1110/ps.9.1.186 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.9.1.186 https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.9.1.186 |
id |
crwiley:10.1110/ps.9.1.186 |
---|---|
record_format |
openpolar |
spelling |
crwiley:10.1110/ps.9.1.186 2024-09-15T18:37:32+00:00 Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 N‐ 1 H NMR spectra Cavagnero, Silvia Thériault, Yves Narula, Surinder S. Dyson, H. Jane Wright, Peter E. 2000 http://dx.doi.org/10.1110/ps.9.1.186 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.9.1.186 https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.9.1.186 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Protein Science volume 9, issue 1, page 186-193 ISSN 0961-8368 1469-896X journal-article 2000 crwiley https://doi.org/10.1110/ps.9.1.186 2024-08-15T04:18:29Z Abstract 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 15 N‐ 1 H 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. Article in Journal/Newspaper Sperm whale Wiley Online Library Protein Science 9 1 186 193 |
institution |
Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
Abstract 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 15 N‐ 1 H 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 |
Article in Journal/Newspaper |
author |
Cavagnero, Silvia Thériault, Yves Narula, Surinder S. Dyson, H. Jane Wright, Peter E. |
spellingShingle |
Cavagnero, Silvia Thériault, Yves Narula, Surinder S. Dyson, H. Jane Wright, Peter E. Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 N‐ 1 H NMR spectra |
author_facet |
Cavagnero, Silvia Thériault, Yves Narula, Surinder S. Dyson, H. Jane Wright, Peter E. |
author_sort |
Cavagnero, Silvia |
title |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 N‐ 1 H NMR spectra |
title_short |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 N‐ 1 H NMR spectra |
title_full |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 N‐ 1 H NMR spectra |
title_fullStr |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 N‐ 1 H NMR spectra |
title_full_unstemmed |
Amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 N‐ 1 H NMR spectra |
title_sort |
amide proton hydrogen exchange rates for sperm whale myoglobin obtained from 15 n‐ 1 h nmr spectra |
publisher |
Wiley |
publishDate |
2000 |
url |
http://dx.doi.org/10.1110/ps.9.1.186 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.9.1.186 https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.9.1.186 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Protein Science volume 9, issue 1, page 186-193 ISSN 0961-8368 1469-896X |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1110/ps.9.1.186 |
container_title |
Protein Science |
container_volume |
9 |
container_issue |
1 |
container_start_page |
186 |
op_container_end_page |
193 |
_version_ |
1810481905147052032 |