| | |
| | |
Stat |
Members: 3645 Articles: 2'501'711 Articles rated: 2609
20 April 2024 |
|
| | | |
|
Article overview
| |
|
Molecular code for cooperativity in hemoglobin | G K Ackers
; M L Doyle
; D Myers
; M A Daugherty
; | Date: |
3 Jan 1992 | Journal: | Science, 255 (5040), 54-63 | Abstract: | Although tetrameric hemoglobin has been studied extensively as a prototype for understanding mechanisms of allosteric regulation, the functional and structural properties of its eight intermediate ligation forms have remained elusive. Recent experiments on the energetics of cooperativity of these intermediates, along with assignments of their quaternary structures, have revealed that the allosteric mechanism is controlled by a previously unrecognized symmetry feature: quaternary switching from form T to form R occurs whenever heme-site binding creates a tetramer with at least one ligated subunit on each dimeric half-molecule. This "symmetry rule" translates the configurational isomers of heme-site ligation into six observed switchpoints of quaternary transition. Cooperativity arises from both "concerted" quaternary switching and "sequential" modulation of binding within each quaternary form, T and R. Binding affinity is regulated through a hierarchical code of tertiary-quaternary coupling that includes the classical allosteric models as limiting cases. | Source: | PubMed, pmid1553532 | Services: | Forum | Review | Favorites |
|
|
No review found.
Did you like this article?
Note: answers to reviews or questions about the article must be posted in the forum section.
Authors are not allowed to review their own article. They can use the forum section.
browser Mozilla/5.0 AppleWebKit/537.36 (KHTML, like Gecko; compatible; ClaudeBot/1.0; +claudebot@anthropic.com)
|
| |
|
|
|
| News, job offers and information for researchers and scientists:
| |