Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix.
The compact, largely helical structure of sperm whale and harbor seal myoglobins undergoes an abrupt one-step transition between pH 4.5 and 3.5 as monitored by changes in either the heme Soret band absorbance or circular dichroism probes of secondary structure, for which a modified Tanford-Kirkwood...
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ftpubmed:oai:pubmedcentral.nih.gov:1327257 2023-05-15T16:33:05+02:00 Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix. Gurd, F R Friend, S H Rothgeb, T M Gurd, R S Scouloudi, H 1980-10 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1327257 http://www.ncbi.nlm.nih.gov/pubmed/7248465 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1327257 http://www.ncbi.nlm.nih.gov/pubmed/7248465 Research Article Text 1980 ftpubmed 2013-08-30T19:11:31Z The compact, largely helical structure of sperm whale and harbor seal myoglobins undergoes an abrupt one-step transition between pH 4.5 and 3.5 as monitored by changes in either the heme Soret band absorbance or circular dichroism probes of secondary structure, for which a modified Tanford-Kirkwood theory provides identification of certain dominant electrostatic interactions responsible for the loss of stability. A similar treatment permits identification of the electrostatic interactions primarily responsible for a process in which the anchoring of the A helix to other parts of the molecule is weakened. This process is detected with both myoglobins, in a pH range approximately 1 unit higher than the onset of the overall unfolding process, through changes in the circular dichroic spectra near 295 nm which correspond to the L1 O-O band of the only two tryptophan residues in these proteins, residues 7 and 14. In each case protonation of certain sites in neighboring parts of the molecule can be identified as producing destabilizing interactions with components of the A helix, particularly with lysine 6. Text harbor seal Sperm whale PubMed Central (PMC) Kirkwood ENVELOPE(-68.975,-68.975,-68.338,-68.338) |
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language |
English |
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Research Article |
spellingShingle |
Research Article Gurd, F R Friend, S H Rothgeb, T M Gurd, R S Scouloudi, H Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix. |
topic_facet |
Research Article |
description |
The compact, largely helical structure of sperm whale and harbor seal myoglobins undergoes an abrupt one-step transition between pH 4.5 and 3.5 as monitored by changes in either the heme Soret band absorbance or circular dichroism probes of secondary structure, for which a modified Tanford-Kirkwood theory provides identification of certain dominant electrostatic interactions responsible for the loss of stability. A similar treatment permits identification of the electrostatic interactions primarily responsible for a process in which the anchoring of the A helix to other parts of the molecule is weakened. This process is detected with both myoglobins, in a pH range approximately 1 unit higher than the onset of the overall unfolding process, through changes in the circular dichroic spectra near 295 nm which correspond to the L1 O-O band of the only two tryptophan residues in these proteins, residues 7 and 14. In each case protonation of certain sites in neighboring parts of the molecule can be identified as producing destabilizing interactions with components of the A helix, particularly with lysine 6. |
format |
Text |
author |
Gurd, F R Friend, S H Rothgeb, T M Gurd, R S Scouloudi, H |
author_facet |
Gurd, F R Friend, S H Rothgeb, T M Gurd, R S Scouloudi, H |
author_sort |
Gurd, F R |
title |
Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix. |
title_short |
Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix. |
title_full |
Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix. |
title_fullStr |
Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix. |
title_full_unstemmed |
Electrostatic stabilization in sperm whale and harbor seal myoglobins. Identification of groups primarily responsible for changes in anchoring of the A helix. |
title_sort |
electrostatic stabilization in sperm whale and harbor seal myoglobins. identification of groups primarily responsible for changes in anchoring of the a helix. |
publishDate |
1980 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1327257 http://www.ncbi.nlm.nih.gov/pubmed/7248465 |
long_lat |
ENVELOPE(-68.975,-68.975,-68.338,-68.338) |
geographic |
Kirkwood |
geographic_facet |
Kirkwood |
genre |
harbor seal Sperm whale |
genre_facet |
harbor seal Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1327257 http://www.ncbi.nlm.nih.gov/pubmed/7248465 |
_version_ |
1766022798456651776 |