HW 1 key - Biological Sciences 102 Homework #1 Keys Spring,...

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Biological Sciences 102 Spring, 2009 Homework #1 Keys Prof R Holland Cheng Learn the structures and the codes of the twenty amino acids ( Table, pp. 78-79, Chapter 4, Garrett & Grisham) 1. Why is it important that weak forces, not strong forces, mediate biomolecular recognition interactions? Biomolecules interact with one another through molecular surfaces that are structurally complementary. How can various proteins interact with molecules as different as simple ions, hydrophobic lipids, polar but uncharged Biochemistry , 3 rd ed., Thomson Brooks/Cole, c2005) Life is a dynamic process characterized by continually changing interactions. Complementary interactions based on covalent bonding would of necessity produce static structures, structures difficult to change and slow to respond to outside stimuli. The amino acid side chains of proteins can participate in a number of interactions through hydrogen bonding, ionic bonding, hydrophobic interactions, and van der Waals interactions. For example, the polar amino acids, acidic amino acids and their amides, and the basic amino acids all have groups that can participate in hydrogen bonding. Those amino acid side chains that have net charge can form ionic bonds. The hydrophobic amino acids can interact with nonpolar, hydrophobic surfaces of molecules. Thus, amino acids are capable of participating in a variety of interactions. A protein can be folded in three dimensions to organize amino acids into surfaces with a range of properties. 2. If the internal pH of a muscle cell is 6.8, what is the [HPO 4 ]/[H 24 ] ratio in this cell? Why do we use the Henderson- Hasselbalch equation to solve this problem? Why do we not just subtract or add molar amounts of acid and base?
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This note was uploaded on 04/19/2009 for the course BIS BIS102 taught by Professor Hilt during the Spring '08 term at UC Davis.

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HW 1 key - Biological Sciences 102 Homework #1 Keys Spring,...

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