The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry
Abstract The unfolding enthalpy of the pH 4 molten globule from sperm whale apomyoglobin has been measured by isothermal titration calorimetry, using titration to acid pH. The unfolding enthalpy is close to zero at 20 °C, in contrast both to the positive values expected for peptide helices and the n...
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crwiley:10.1110/ps.9.7.1340 2024-06-02T08:14:53+00:00 The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry Jamin, Marc Loh, Stewart N. Baldwin, Robert L. Antalik, Marian Bolen, D. Wayne Loh, Stewart N. 2000 http://dx.doi.org/10.1110/ps.9.7.1340 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.9.7.1340 https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.9.7.1340 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Protein Science volume 9, issue 7, page 1340-1346 ISSN 0961-8368 1469-896X journal-article 2000 crwiley https://doi.org/10.1110/ps.9.7.1340 2024-05-03T11:39:03Z Abstract The unfolding enthalpy of the pH 4 molten globule from sperm whale apomyoglobin has been measured by isothermal titration calorimetry, using titration to acid pH. The unfolding enthalpy is close to zero at 20 °C, in contrast both to the positive values expected for peptide helices and the negative values reported for holomyoglobin and native apomyoglobin. At 20 °C, the hydrophobic interaction should make only a small contribution to the unfolding enthalpy according to the liquid hydrocarbon model. Our result indicates that some factor present in the unfolding enthalpies of native proteins makes the unfolding enthalpy of the pH 4 molten globule less positive than expected from data for peptide helices. Article in Journal/Newspaper Sperm whale Wiley Online Library Protein Science 9 7 1340 1346 |
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Wiley Online Library |
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English |
description |
Abstract The unfolding enthalpy of the pH 4 molten globule from sperm whale apomyoglobin has been measured by isothermal titration calorimetry, using titration to acid pH. The unfolding enthalpy is close to zero at 20 °C, in contrast both to the positive values expected for peptide helices and the negative values reported for holomyoglobin and native apomyoglobin. At 20 °C, the hydrophobic interaction should make only a small contribution to the unfolding enthalpy according to the liquid hydrocarbon model. Our result indicates that some factor present in the unfolding enthalpies of native proteins makes the unfolding enthalpy of the pH 4 molten globule less positive than expected from data for peptide helices. |
format |
Article in Journal/Newspaper |
author |
Jamin, Marc Loh, Stewart N. Baldwin, Robert L. Antalik, Marian Bolen, D. Wayne Loh, Stewart N. |
spellingShingle |
Jamin, Marc Loh, Stewart N. Baldwin, Robert L. Antalik, Marian Bolen, D. Wayne Loh, Stewart N. The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry |
author_facet |
Jamin, Marc Loh, Stewart N. Baldwin, Robert L. Antalik, Marian Bolen, D. Wayne Loh, Stewart N. |
author_sort |
Jamin, Marc |
title |
The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry |
title_short |
The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry |
title_full |
The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry |
title_fullStr |
The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry |
title_full_unstemmed |
The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry |
title_sort |
unfolding enthalpy of the ph 4 molten globule of apomyoglobin measured by isothermal titration calorimetry |
publisher |
Wiley |
publishDate |
2000 |
url |
http://dx.doi.org/10.1110/ps.9.7.1340 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1110%2Fps.9.7.1340 https://onlinelibrary.wiley.com/doi/pdf/10.1110/ps.9.7.1340 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Protein Science volume 9, issue 7, page 1340-1346 ISSN 0961-8368 1469-896X |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1110/ps.9.7.1340 |
container_title |
Protein Science |
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9 |
container_issue |
7 |
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1340 |
op_container_end_page |
1346 |
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1800738882357035008 |