基因的分子生物学英文版答案molecular chapter5.pdfVIP

Chapter 5 Answers 1. The 20 amino acids used for protein synthesis can be divided into four general categories, based upon the chemical properties of their side chains. The four categories are neutral-nonpolar (with side chains composed of simple carbon chains or aromatic rings), neutral-polar (including hydroxyl, sulfhydryl, amide, and imidazole moieties), basic (with side chains including primary and secondary amines), and acidic (with side chains including carboxylates). The type of interaction made by each of the amino acids reflects the chemical nature of its side chain. For example, the neutral-nonpolar side chains generally make hydrophobic contacts with other molecules, and the neutral-polar side chains most commonly participate in hydrogen bond interactions. Similarly, the charged (acidic and basic) side chains interact via ionic or hydrogen bonds. Finally, all four types of side chains can make van der Waals contacts, as these depend only on the nearby presence of other atoms and not on the chemical properties of the involved groups. 2. Primary structure refers to the linear sequence of amino acids within a polypeptide chain. Accordingly, every protein has a primary structure, consisting simply of its amino acid sequence. Secondary structure refers to the local structures that are formed by stretches of amino acids within a polypeptide chain. The most common secondary structural elements are the  helix and the  sheet. Tertiary structure refers to the overall three-dimensional structure of a polypeptide chain. A tertiary structure includes all of the secondary structural elements present within the polypeptide. An example of a tertiary structure is shown in Figure 5-26, indicating the distinct cAMP binding and DNA-binding domains of the CAP protein. Quarternary structure refers to the way in which multiple polypeptide subunits interact with each other to form a protein complex —fo