By Fuyuhiko Tamanoi
Content material: quantity I: constitution and keep an eye on. -- quantity II: Kinetics and mechanism
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5 A. Charged residues such as aspartic acid would not be accommodated because of the highly hydrophobic nature of the a2 binding surface. These results are consistent with FTase peptide substrate specificity {38). The side-chain of the ai residue of the Caia2X peptide is exposed to solvent (Figs. 7 and 10) and can easily accommodate a variety of amino acids. FTase shows Httle selectivity for this residue, but Caia2X peptides with amino acids that tend to disrupt backbone structure, such as proline and glycine, at the ai position have lower affinity {38).
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