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By Devita V.T.
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Sample text
MEMBRANE PROTEINS Proteins interact with membranes using a variety of mechanisms. Integral membrane proteins contain amino acid residues with hydrophobic side chains that interact with the fatty acyl groups of the membrane phospholipids. Other integral proteins contain covalently bound fatty acids that function as anchors in the hydrophobic lipid bilayer. An important example is the farnesyl residue of the oncogene p21 ras (the mutant of the normal cellular small g protein) and the myristate residue of the v-src tyrosine kinase oncogene (the mutant of the normal cellular protein c-src).
As noted earlier, G hydrogen-bonds specifically with a C, whereas an A can only hydrogen-bond with a T. The resulting base pairs are said to be complementary. As shown in Figure 1-3, the GC base pair has three hydrogen bonds, and the AT base pair has only two hydrogen bonds. Each strand can serve as the template for the synthesis of the other, enabling faithful reproduction of the genetic code. FIGURE 1-3. Base pairs are formed by hydrogen bonds. T=A; GºC. The two polynucleotide chains of the DNA double helix run in opposite directions (antiparallel).
FIGURE 1-7. Control points in cellular regulation that can be targets for carcinogenic events. The following classes can become oncogenes: growth factors (I), receptors (II), transducers (III), and gene regulation factors (IV). mRNA, messenger RNA. A third class of receptors is the G protein–linked receptors. These sensors indirectly activate or inactivate a separate membrane-bound enzyme or ion channel. The interaction takes place through an intermediary protein, the GTP-binding regulatory protein (G protein).