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- W2063711314 abstract "Bovine brain calmodulin binds 3 mol aluminum per mol protein with dissociation constants in the range of 10−7 to 10−6 molar. EPR spectra of spin-labelled calmodulin provide data indicating that aluminum binding causes decreased probe immobilization as compared to the effects of calcium binding. This result of aluminum binding indicates that Al-calmodulin is a more random, open polypeptide relative to the structure of Ca2+-calmodulin. Calorimetric measurements of aluminum binding provide data showing that the first mol of aluminum bound is accompanied by the largest enthalpic change (−3.9 kcal mol−1), whereas binding of the second and third mol of aluminum are each entropically driven." @default.
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- W2063711314 date "1983-09-01" @default.
- W2063711314 modified "2023-10-14" @default.
- W2063711314 title "A thermodynamic and electron paramagnetic resonance study of structural changes in calmodulin induced by aluminum binding" @default.
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- W2063711314 doi "https://doi.org/10.1016/s0006-291x(83)80174-0" @default.
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