Conformational free energies of myoglobins of small mammals
Myoglobins from three small placental mammals and one small marsupial were isolated from cardiac or skeletal muscle. The conformational free energies of these four myoglobins were estimated from guanidinium chloride unfolding data at pH 8 and 25°. The myoglobins from rat and rabbit are more stable t...
Published in: | International Journal of Peptide and Protein Research |
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crwiley:10.1111/j.1399-3011.1988.tb00035.x 2024-06-02T08:14:52+00:00 Conformational free energies of myoglobins of small mammals KELLY, LENORE SIMMONS, JOE H. HECK, TERRY HOLLADAY, LESLIE A. 1988 http://dx.doi.org/10.1111/j.1399-3011.1988.tb00035.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1399-3011.1988.tb00035.x https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3011.1988.tb00035.x en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor International Journal of Peptide and Protein Research volume 31, issue 3, page 281-288 ISSN 0367-8377 journal-article 1988 crwiley https://doi.org/10.1111/j.1399-3011.1988.tb00035.x 2024-05-03T11:44:28Z Myoglobins from three small placental mammals and one small marsupial were isolated from cardiac or skeletal muscle. The conformational free energies of these four myoglobins were estimated from guanidinium chloride unfolding data at pH 8 and 25°. The myoglobins from rat and rabbit are more stable than that of the most stable myoglobin previously studied, that of the sperm whale. In addition, these two myoglobins unfold with greater cooperativity than previously characterized myoglobins. The data obtained herein demonstrate unequivocally for the first time that the stability of homeotherm myoglobins correlates with neither the size of the organism nor its metabolic rate. Article in Journal/Newspaper Sperm whale Wiley Online Library International Journal of Peptide and Protein Research 31 3 281 288 |
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Open Polar |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Myoglobins from three small placental mammals and one small marsupial were isolated from cardiac or skeletal muscle. The conformational free energies of these four myoglobins were estimated from guanidinium chloride unfolding data at pH 8 and 25°. The myoglobins from rat and rabbit are more stable than that of the most stable myoglobin previously studied, that of the sperm whale. In addition, these two myoglobins unfold with greater cooperativity than previously characterized myoglobins. The data obtained herein demonstrate unequivocally for the first time that the stability of homeotherm myoglobins correlates with neither the size of the organism nor its metabolic rate. |
format |
Article in Journal/Newspaper |
author |
KELLY, LENORE SIMMONS, JOE H. HECK, TERRY HOLLADAY, LESLIE A. |
spellingShingle |
KELLY, LENORE SIMMONS, JOE H. HECK, TERRY HOLLADAY, LESLIE A. Conformational free energies of myoglobins of small mammals |
author_facet |
KELLY, LENORE SIMMONS, JOE H. HECK, TERRY HOLLADAY, LESLIE A. |
author_sort |
KELLY, LENORE |
title |
Conformational free energies of myoglobins of small mammals |
title_short |
Conformational free energies of myoglobins of small mammals |
title_full |
Conformational free energies of myoglobins of small mammals |
title_fullStr |
Conformational free energies of myoglobins of small mammals |
title_full_unstemmed |
Conformational free energies of myoglobins of small mammals |
title_sort |
conformational free energies of myoglobins of small mammals |
publisher |
Wiley |
publishDate |
1988 |
url |
http://dx.doi.org/10.1111/j.1399-3011.1988.tb00035.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1399-3011.1988.tb00035.x https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1399-3011.1988.tb00035.x |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
International Journal of Peptide and Protein Research volume 31, issue 3, page 281-288 ISSN 0367-8377 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1111/j.1399-3011.1988.tb00035.x |
container_title |
International Journal of Peptide and Protein Research |
container_volume |
31 |
container_issue |
3 |
container_start_page |
281 |
op_container_end_page |
288 |
_version_ |
1800738875634614272 |