Controlling water pollution in construction.
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Construction Materials↗
Biomedical subjects
A McAlpine
Publications and source records attributed to A McAlpine.
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Calorimetric studies of the energetics of protein-DNA interactions in the E. coli methionine repressor (MetJ) system.
Calorimetric measurements of binding of a specific DNA fragment and S-adenosyl methionine (SAM) co-repressor molecules to the E. coli methionine repressor (MetJ) show significant differences in the energetics of binary and ternary protein-DNA complexes. Formation of the MetJ:SAM:DNA ternary complex is significantly more exothermic (delta H congruent to -99 kJ.mol-1) than either MetJ:DNA or MetJ:SAM binary complexes alone (delta H congruent to -10 kJ.mol-1 each). The protein is also significantly more stable to unfolding (delta Tm congruent to 5.4 degrees C) when bound to DNA. These observations suggest that binding of SAM to the protein-DNA complex leads to a significant reduction in dynamic flexibility of the ternary complex, with considerable entropy-enthalpy compensation, not necessarily involving any overall conformational change.
Bacterial Proteins↗
Structure of the thromboxane receptor antagonist EP 092.
7-(3-[1-(4-Phenylthiosemicarbazono)ethyl]-bicyclo[2.2.1]hept-2- yl)-5-heptenoic acid, C23H31N3-O2S, Mr = 413.7, monoclinic, P2(1)/a, a = 12.9650 (7), b = 11.2081 (6), c = 16.8941 (12) A, beta = 110.452 (5) degrees, V = 2300.2 A3, Z = 4, Dx = 1.194 g cm-3, Mo K alpha, lambda = 0.71073 A, mu = 1.55 cm-1, F(000) = 888, T = 298 K. Final R = 0.0472 with 2778 independent data. EP 092 is a thromboxane receptor antagonist akin to many other analogues of the thromboxane A2 [Wilson & Jones (1985). Adv. Prostaglandin Thromboxane Leukotriene Res. 14, 393-425].
Molecular Conformation↗