Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding
Reaction of the Schiff-base complex [Co(acetylacetonate-ethylenediimine)(NH3)(2)](+) with metmyoglobin at pH 6.5 yields a partially folded protein containing six Co(III) complexes. Although half of its a-helical secondary structure is retained, absorption and Co spectra indicate that the tertiary st...
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National Academy of Sciences
1998
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ftcaltechauth:oai:authors.library.caltech.edu:4yvy5-6gq07 2024-06-23T07:56:58+00:00 Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding Blum, Ofer Haiek, Abed Cwikel, Dory Dori, Zvi Meade, Thomas J. Gray, Harry B. 1998-06-09 https://www.ncbi.nlm.nih.gov/pmc/PMC22589 unknown National Academy of Sciences http://www.pnas.org/cgi/content/abstract/95/12/6659 oai:authors.library.caltech.edu:4yvy5-6gq07 https://www.ncbi.nlm.nih.gov/pmc/PMC22589 eprintid:603 resolverid:CaltechAUTHORS:BLUpnas98 info:eu-repo/semantics/openAccess Other Proceedings of the National Academy of Sciences of the United States of America, 95(12), 6659-6662, (1998-06-09) protein unfolding cobalt complexes SPERM WHALE MYOGLOBIN CYTOCHROME-C INTERMEDIATE APOMYOGLOBIN PATHWAY ACID STABILITY STATES HORSE info:eu-repo/semantics/article 1998 ftcaltechauth 2024-06-12T06:12:34Z Reaction of the Schiff-base complex [Co(acetylacetonate-ethylenediimine)(NH3)(2)](+) with metmyoglobin at pH 6.5 yields a partially folded protein containing six Co(III) complexes. Although half of its a-helical secondary structure is retained, absorption and Co spectra indicate that the tertiary structure in both B-F and AGH domains is disrupted in the partially folded protein. In analogy to proton-induced unfolding, it is likely that the loss of tertiary structure is triggered by metal-ion binding to histidines. Cobalt(III)-induced unfolding of myoglobin is unique in its selectivity (other proteins are unaffected) and in allowing the isolation of the partially folded macromolecule (the protein does not refold or aggregate upon removal of free denaturant). © 1998 by The National Academy of Sciences. Contributed by Harry B. Gray, April 6, 1998. We thank Drs. Bassil Dahiyat and Michel E. Goldberg for discussions. O.B. acknowledges Rothchild and Fulbright postdoctoral fellowships. This work was supported by the National Science Foundation, the Arnold and Mabel Beckman Foundation, and the Redox Pharmaceutical Corporation. Published - BLUpnas98.pdf Article in Journal/Newspaper Sperm whale Caltech Authors (California Institute of Technology) Mabel ENVELOPE(-44.683,-44.683,-60.667,-60.667) |
institution |
Open Polar |
collection |
Caltech Authors (California Institute of Technology) |
op_collection_id |
ftcaltechauth |
language |
unknown |
topic |
protein unfolding cobalt complexes SPERM WHALE MYOGLOBIN CYTOCHROME-C INTERMEDIATE APOMYOGLOBIN PATHWAY ACID STABILITY STATES HORSE |
spellingShingle |
protein unfolding cobalt complexes SPERM WHALE MYOGLOBIN CYTOCHROME-C INTERMEDIATE APOMYOGLOBIN PATHWAY ACID STABILITY STATES HORSE Blum, Ofer Haiek, Abed Cwikel, Dory Dori, Zvi Meade, Thomas J. Gray, Harry B. Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding |
topic_facet |
protein unfolding cobalt complexes SPERM WHALE MYOGLOBIN CYTOCHROME-C INTERMEDIATE APOMYOGLOBIN PATHWAY ACID STABILITY STATES HORSE |
description |
Reaction of the Schiff-base complex [Co(acetylacetonate-ethylenediimine)(NH3)(2)](+) with metmyoglobin at pH 6.5 yields a partially folded protein containing six Co(III) complexes. Although half of its a-helical secondary structure is retained, absorption and Co spectra indicate that the tertiary structure in both B-F and AGH domains is disrupted in the partially folded protein. In analogy to proton-induced unfolding, it is likely that the loss of tertiary structure is triggered by metal-ion binding to histidines. Cobalt(III)-induced unfolding of myoglobin is unique in its selectivity (other proteins are unaffected) and in allowing the isolation of the partially folded macromolecule (the protein does not refold or aggregate upon removal of free denaturant). © 1998 by The National Academy of Sciences. Contributed by Harry B. Gray, April 6, 1998. We thank Drs. Bassil Dahiyat and Michel E. Goldberg for discussions. O.B. acknowledges Rothchild and Fulbright postdoctoral fellowships. This work was supported by the National Science Foundation, the Arnold and Mabel Beckman Foundation, and the Redox Pharmaceutical Corporation. Published - BLUpnas98.pdf |
format |
Article in Journal/Newspaper |
author |
Blum, Ofer Haiek, Abed Cwikel, Dory Dori, Zvi Meade, Thomas J. Gray, Harry B. |
author_facet |
Blum, Ofer Haiek, Abed Cwikel, Dory Dori, Zvi Meade, Thomas J. Gray, Harry B. |
author_sort |
Blum, Ofer |
title |
Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding |
title_short |
Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding |
title_full |
Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding |
title_fullStr |
Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding |
title_full_unstemmed |
Isolation of a myoglobin molten globule by selective cobalt(III)-induced unfolding |
title_sort |
isolation of a myoglobin molten globule by selective cobalt(iii)-induced unfolding |
publisher |
National Academy of Sciences |
publishDate |
1998 |
url |
https://www.ncbi.nlm.nih.gov/pmc/PMC22589 |
long_lat |
ENVELOPE(-44.683,-44.683,-60.667,-60.667) |
geographic |
Mabel |
geographic_facet |
Mabel |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_source |
Proceedings of the National Academy of Sciences of the United States of America, 95(12), 6659-6662, (1998-06-09) |
op_relation |
http://www.pnas.org/cgi/content/abstract/95/12/6659 oai:authors.library.caltech.edu:4yvy5-6gq07 https://www.ncbi.nlm.nih.gov/pmc/PMC22589 eprintid:603 resolverid:CaltechAUTHORS:BLUpnas98 |
op_rights |
info:eu-repo/semantics/openAccess Other |
_version_ |
1802650391154786304 |