Stability characteristics of deuterated myoglobin
Abstract Purified sperm whale myoglobin was deuterated by being exposed to pD 3.5 in D 2 O buffer for 1 hr, then raised to pD 10.6 for an additional hour, and finally brought to neutrality in a D 2 O environment. Control myoglobin was similarly treated in H 2 O. The specific rotation at 233 mμ and/o...
Published in: | Biopolymers |
---|---|
Main Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
1971
|
Subjects: | |
Online Access: | http://dx.doi.org/10.1002/bip.360101122 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.360101122 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.360101122 |
id |
crwiley:10.1002/bip.360101122 |
---|---|
record_format |
openpolar |
spelling |
crwiley:10.1002/bip.360101122 2024-06-02T08:14:53+00:00 Stability characteristics of deuterated myoglobin Appel, Pearl Brown, W. Duane 1971 http://dx.doi.org/10.1002/bip.360101122 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.360101122 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.360101122 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Biopolymers volume 10, issue 11, page 2309-2322 ISSN 0006-3525 1097-0282 journal-article 1971 crwiley https://doi.org/10.1002/bip.360101122 2024-05-03T11:38:55Z Abstract Purified sperm whale myoglobin was deuterated by being exposed to pD 3.5 in D 2 O buffer for 1 hr, then raised to pD 10.6 for an additional hour, and finally brought to neutrality in a D 2 O environment. Control myoglobin was similarly treated in H 2 O. The specific rotation at 233 mμ and/or the absorbance in the Soret region were used to follow the helix‐coil transition of myoglobin subjected to denaturation by acid, alkali, urea and guanidine. Deuterated and control myoglobin had similar 50% transition points in the four denaturing media studied (acid: pH 4.4, pD 4.9; alkali: pH 9.4, pD 10.0; urea, 7.2 M guanidine, 2.5 M ). The shift toward the alkaline side of 0.5 or 0.6 units of the transition induced by either acid or alkaline denaturation reflects only the weakened acidity of ionizable groups in deuterium systems. Deuterated myoglobin in 3.25 M guanidine had a 20% faster denaturation rate than that of control. Acid, urea, and guanidine denaturation curves showed fairly steep transitions, taken as indicative of a one‐step process involving only two states (native and denatured molecules). Supporting this conclusion was the fact that plots of absorption and polarimetry measurements of the helix‐coil transition induced by either acid or guanidine could be superimposed. Article in Journal/Newspaper Sperm whale Wiley Online Library Biopolymers 10 11 2309 2322 |
institution |
Open Polar |
collection |
Wiley Online Library |
op_collection_id |
crwiley |
language |
English |
description |
Abstract Purified sperm whale myoglobin was deuterated by being exposed to pD 3.5 in D 2 O buffer for 1 hr, then raised to pD 10.6 for an additional hour, and finally brought to neutrality in a D 2 O environment. Control myoglobin was similarly treated in H 2 O. The specific rotation at 233 mμ and/or the absorbance in the Soret region were used to follow the helix‐coil transition of myoglobin subjected to denaturation by acid, alkali, urea and guanidine. Deuterated and control myoglobin had similar 50% transition points in the four denaturing media studied (acid: pH 4.4, pD 4.9; alkali: pH 9.4, pD 10.0; urea, 7.2 M guanidine, 2.5 M ). The shift toward the alkaline side of 0.5 or 0.6 units of the transition induced by either acid or alkaline denaturation reflects only the weakened acidity of ionizable groups in deuterium systems. Deuterated myoglobin in 3.25 M guanidine had a 20% faster denaturation rate than that of control. Acid, urea, and guanidine denaturation curves showed fairly steep transitions, taken as indicative of a one‐step process involving only two states (native and denatured molecules). Supporting this conclusion was the fact that plots of absorption and polarimetry measurements of the helix‐coil transition induced by either acid or guanidine could be superimposed. |
format |
Article in Journal/Newspaper |
author |
Appel, Pearl Brown, W. Duane |
spellingShingle |
Appel, Pearl Brown, W. Duane Stability characteristics of deuterated myoglobin |
author_facet |
Appel, Pearl Brown, W. Duane |
author_sort |
Appel, Pearl |
title |
Stability characteristics of deuterated myoglobin |
title_short |
Stability characteristics of deuterated myoglobin |
title_full |
Stability characteristics of deuterated myoglobin |
title_fullStr |
Stability characteristics of deuterated myoglobin |
title_full_unstemmed |
Stability characteristics of deuterated myoglobin |
title_sort |
stability characteristics of deuterated myoglobin |
publisher |
Wiley |
publishDate |
1971 |
url |
http://dx.doi.org/10.1002/bip.360101122 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbip.360101122 https://onlinelibrary.wiley.com/doi/pdf/10.1002/bip.360101122 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Biopolymers volume 10, issue 11, page 2309-2322 ISSN 0006-3525 1097-0282 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/bip.360101122 |
container_title |
Biopolymers |
container_volume |
10 |
container_issue |
11 |
container_start_page |
2309 |
op_container_end_page |
2322 |
_version_ |
1800738895077310464 |