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- W324271808 abstract "This chapter discusses about subunit interactions in allosteric control. Cooperative effects were originally discovered in hemoglobin and have been shown to be a characteristic of most regulatory proteins. To understand the ligand-induced changes of a protein molecule it is necessary to develop diagnostic methods. It is apparent that a quantitative evaluation of the intrinsic constants of ligand binding can lead to a diagnosis between models and therefore can provide insight into the strength of the individual molecular parameters. Ligand-induced conformational changes are required to explain negative cooperativity apparent in many proteins. They are required to explain the physical changes indicated in a positively cooperative system like hemoglobin. It appears that many other processes—the peeling of a repressor from DNA, the change in a transport protein on a membrane, the reaction of a nerve receptor—are similar in nature and involve induced conformational changes." @default.
- W324271808 created "2016-06-24" @default.
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- W324271808 date "1972-01-01" @default.
- W324271808 modified "2023-09-26" @default.
- W324271808 title "SUBUNIT INTERACTIONS IN ALLOSTERIC CONTROL" @default.
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- W324271808 doi "https://doi.org/10.1016/b978-0-08-016874-6.50023-0" @default.
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