The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry.
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 degrees C, in contrast both to the positive values expected for peptide helices and the neg...
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ftpubmed:oai:pubmedcentral.nih.gov:2144672 2023-05-15T18:26:42+02:00 The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry. Jamin, M. Antalik, M. Loh, S. N. Bolen, D. W. Baldwin, R. L. 2000-07 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144672 http://www.ncbi.nlm.nih.gov/pubmed/10933499 en eng Cold Spring Harbor Laboratory Press http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144672 http://www.ncbi.nlm.nih.gov/pubmed/10933499 Research Article Text 2000 ftpubmed 2013-09-01T10:32:16Z 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 degrees C, in contrast both to the positive values expected for peptide helices and the negative values reported for holomyoglobin and native apomyoglobin. At 20 degrees 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. Text Sperm whale PubMed Central (PMC) |
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Research Article Jamin, M. Antalik, M. Loh, S. N. Bolen, D. W. Baldwin, R. L. The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry. |
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Research Article |
description |
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 degrees C, in contrast both to the positive values expected for peptide helices and the negative values reported for holomyoglobin and native apomyoglobin. At 20 degrees 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 |
Text |
author |
Jamin, M. Antalik, M. Loh, S. N. Bolen, D. W. Baldwin, R. L. |
author_facet |
Jamin, M. Antalik, M. Loh, S. N. Bolen, D. W. Baldwin, R. L. |
author_sort |
Jamin, M. |
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 |
Cold Spring Harbor Laboratory Press |
publishDate |
2000 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144672 http://www.ncbi.nlm.nih.gov/pubmed/10933499 |
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Sperm whale |
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Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2144672 http://www.ncbi.nlm.nih.gov/pubmed/10933499 |
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1766208674607398912 |