BIOC 3560 Lecture 4: biochem PACK FOUR.pdf
3 Dec 2014
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Chemical energy p. 179-181; 182-184 problem #7, p. 185. Review: in globins, steric hindrance and a h-bond between his e7 and o2 (thermodynamically favourable) improve the specificity of binding to o2. Selectivity is not perfect, however, and co binds with higher affinity, but not as high as to free heme. Myoglobin binds o2 with high affinity, and for a wide range of po2 it is relatively insensitive to changes in po2. At the po2 of tissues (~ 4 kpa), it is nearly saturated. Structure of globins ii: hemoglobin myoglobin subunit of hemoglobin. Comparing globin sequences position: f1 f2 f3 f4 f5 f6 f7 f8 f9 globin. Mb: leu ser ala leu ser asp leu his ala. Hb: phe ala thr leu ser glu leu his ala. Hb: leu lys pro leu ala gln ser his cys. In different globins, segments of (mostly) different amino acids form similar structures.
