For each of the following amino acids: 1) describe what the important functional group of the amino acid side chain is, 2) identify the charge of the side chain, 3) name another component in the structure that the amino acid might interact with, and 4) indicate how the interaction with the component listed in 3) might be occurring (i.e., electrostatic interaction, hydrogen bond, hydrophobic interaction, etc.) a) Asp153 b) Arg166 c) Lys167

Which of the following types of molecular interactions play a role in protein folding? Select all that apply. A.)Hydrophobic interactions B.)Van der Waals attraction C.)Hydrogen bonds D.)Covalent bonds

The isoelectric point of an amino acid is the point where; O a) the amino acid carries no net electrical charge b) the a-carboxylic acid is protonated and the a-amino group is unprotonated c) ) the pKa of the a-carboxylic acid is the same as the pK, of the a-amino group a d) the solubility of the amino acid is maximized e) the a-carboxylic acid and the a-amino group are both half protonated MacBo 80 000 esc F1 F2 F3 F4

Which type of amino acid would you expect to find in large numbers in a protein found in a deep-sea hydrothermal vent (a very hot environment)? A.)Polar amino acids B.)Cysteines C.)Hydrophobic amino acids D.)Nonpolar amino acids

Protein denaturation usually refers to the disruption of which of the following types of molecular interactions? Select all that apply. A.)Van der Waals attraction B.)Covalent bonds C.)Hydrogen bonds D.)Hydrophobic interactions

Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.

b) The likelihood of both triglycerides and phospholipids to behave as liquids at a given temperature is affected by their degree of saturation. Explain what saturation is and provide a biochemical explanation for why it affects the likelihood of a lipid to behave as a liquid at a given temperature. 5) a) Proteins have multiple "levels" of structural complexity. Match the type of chemical bond on the left with the level of protein structure that they are specifically involved in maintaining on the right. (Note that more than one letter may apply to each structural level and that each letter may be used more than once or not at all). a. disulphide bonds Tertiary structure b. hydrogen bonds Primary structure c. ionic bonds Quaternary structure d. peptide bonds Secondary structure