Allosteric modulation of monomeric proteins*
Abstract Multimeric proteins ( e.g. hemoglobin) are considered to be the prototypes of allosteric enzymes, whereas monomeric proteins ( e.g. myoglobin) usually are assumed to be nonallosteric. However, the modulation of the functional properties of monomeric proteins by heterotropic allosteric effec...
| Published in: | Biochemistry and Molecular Biology Education |
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| Main Authors: | , , , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
2005
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1002/bmb.2005.494033032470 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fbmb.2005.494033032470 https://iubmb.onlinelibrary.wiley.com/doi/pdf/10.1002/bmb.2005.494033032470 |
| Summary: | Abstract Multimeric proteins ( e.g. hemoglobin) are considered to be the prototypes of allosteric enzymes, whereas monomeric proteins ( e.g. myoglobin) usually are assumed to be nonallosteric. However, the modulation of the functional properties of monomeric proteins by heterotropic allosteric effectors casts doubts on this assumption. Here, the allosteric properties of sperm whale myoglobin, human serum albumin, and human α‐thrombin, generally considered as molecular models of monomeric proteins, are summarized. |
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