Stabilization of myoglobin by multiple alanine substitutions in helical positions.
We have carried out a series of multiple Xaa-->Ala changes at nonadjacent surface positions in the sequence of sperm whale myoglobin. Although the corresponding single substitutions do not increase the thermal stability of the protein, multiple substitutions enhance the stability of the resulting...
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Cold Spring Harbor Laboratory Press
1994
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ftpubmed:oai:pubmedcentral.nih.gov:2142936 2023-05-15T18:26:43+02:00 Stabilization of myoglobin by multiple alanine substitutions in helical positions. Lin, L. Pinker, R. J. Phillips, G. N. Kallenbach, N. R. 1994-09 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142936 http://www.ncbi.nlm.nih.gov/pubmed/7833805 en eng Cold Spring Harbor Laboratory Press http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142936 http://www.ncbi.nlm.nih.gov/pubmed/7833805 Research Article Text 1994 ftpubmed 2013-09-01T10:26:52Z We have carried out a series of multiple Xaa-->Ala changes at nonadjacent surface positions in the sequence of sperm whale myoglobin. Although the corresponding single substitutions do not increase the thermal stability of the protein, multiple substitutions enhance the stability of the resulting myoglobins. The effect observed is an increase in the observed Tm (midpoint unfolding temperature) relative to that predicted from assuming additivity of the free energy changes corresponding to single mutations. The stabilization occurs in the presence of urea, as measured by the dependence of the unfolding temperature on urea concentration. The sites that have been altered occur in different helices and are not close in sequence or in the native structure of myoglobin. The observed effect is consistent with a role of multiple alanines in residual interactions in the unfolded state of the mutant proteins. Text Sperm whale PubMed Central (PMC) |
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Research Article Lin, L. Pinker, R. J. Phillips, G. N. Kallenbach, N. R. Stabilization of myoglobin by multiple alanine substitutions in helical positions. |
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Research Article |
description |
We have carried out a series of multiple Xaa-->Ala changes at nonadjacent surface positions in the sequence of sperm whale myoglobin. Although the corresponding single substitutions do not increase the thermal stability of the protein, multiple substitutions enhance the stability of the resulting myoglobins. The effect observed is an increase in the observed Tm (midpoint unfolding temperature) relative to that predicted from assuming additivity of the free energy changes corresponding to single mutations. The stabilization occurs in the presence of urea, as measured by the dependence of the unfolding temperature on urea concentration. The sites that have been altered occur in different helices and are not close in sequence or in the native structure of myoglobin. The observed effect is consistent with a role of multiple alanines in residual interactions in the unfolded state of the mutant proteins. |
format |
Text |
author |
Lin, L. Pinker, R. J. Phillips, G. N. Kallenbach, N. R. |
author_facet |
Lin, L. Pinker, R. J. Phillips, G. N. Kallenbach, N. R. |
author_sort |
Lin, L. |
title |
Stabilization of myoglobin by multiple alanine substitutions in helical positions. |
title_short |
Stabilization of myoglobin by multiple alanine substitutions in helical positions. |
title_full |
Stabilization of myoglobin by multiple alanine substitutions in helical positions. |
title_fullStr |
Stabilization of myoglobin by multiple alanine substitutions in helical positions. |
title_full_unstemmed |
Stabilization of myoglobin by multiple alanine substitutions in helical positions. |
title_sort |
stabilization of myoglobin by multiple alanine substitutions in helical positions. |
publisher |
Cold Spring Harbor Laboratory Press |
publishDate |
1994 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142936 http://www.ncbi.nlm.nih.gov/pubmed/7833805 |
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Sperm whale |
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Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2142936 http://www.ncbi.nlm.nih.gov/pubmed/7833805 |
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1766208688162340864 |