1. At pH 7, the net charge of lysine is А. -2 В. -1 С. 0 D. +1 Е. +2
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- The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.2- Some proteins contain additional amino acids that arise by modification of an amino acid already present in a peptide , examples include: a) Gamma Amino Butyric Acid. b) 5 - hydroxy Lysine c) 4 - hydroxy proline d) All of the above e) None of the above3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule
- 4. Which best describes the contribution of quaternary (4’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino B) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence acid side chains of amino acids from beginning to end of molecule1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) CondensationWhat is the primary reason the a-helix conformation in polypeptides such a stable form? A. The a-helix structure is stabilized by hydrophobic interactions. B. The a-helix structure is stabilized by intra-helical hydrogen bonds. C. The a-helix structure is stabilized by disulfide bonds. D. The a-helix structure is stabilized by proline residues.
- The R-group of lysine has an overall positive charge. The R-group of glutamic acid has an overall negative charge. Within the structure of a protein molecule, these two amino acids will: O attract each other O repel each other O form a disulfide bridge O form a pure covalent bondWhich of the following statement about proteins is correct a. alpha helix and Beta pleated sheets are considered quaternary structures b. a single polypeptide only has primary sytructure, secondary, tertiary, and quaternary structures require more than one polypeptide c. there are 30 essential amino acids that are the monomer building blocks of proteins d. polypeptides have a distinct polarity (directionality) with one end refered to as the free amino end, and the other called the free carboxyl end6.All of the following types of interactions cooperate in stabilizing the tertiary structures of globular proteins except____. a.Disulphide bond b.Hydrogen bond c.Ionic interactions d.Peptide bond
- 1. Methionine is an amino acid that contains a ___. *a. sodium atomb. sulfur atomc. phenyl ringd. heterocyclic ringe. chlorine atom 2. Which of the following shows all of the tripeptides that can be formed from one molecule each of glycine (Gly), valine (Val), and leucine (Leu)? *a. Gly-Val-Leu, Gly-Leu-Val, Leu-Gly-Valb. Val-Gly-Leu, Gly-Val-Leu, Gly-Leu-Val, Leu-Gly-Valc. Gly-Val-Leu, Gly-Leu-Val, Val-Leu-Gly, Val-Gly-Leu, Leu-Gly-Val, Leu-Val-Glyd. Val-Gly-Leu, Gly-Leu-Vale. Gly-Val-Leu 3. Two amino groups are present in ___. *a. leucineb. Lysinec. Glutamic acidd. threonineVDAATFKQANDNG” is the sequence of an α helix. Which of the following interactions is probable? (... denotes a H-bond) N...A F...V V...A Q...AA. A solution of amino acid having carboxylic side chain was titrated against NaOH. If the initial pH of the solution was 2.8. Describe the state of the functional groups of the amino acid at the initial pH and at 10.5 B. Briefly explain how you will separate amino acid mixture using the change difference between amino acids. C.A given glycine solution was titrated against NaOH and pH of the final solution was 4.8. Given that pKa1 and pKa2 of the glycine are 2.34 and 9.60 respectivel. Calculate the concentration of the dissociated amino acid in terms of the undissociated amino acid. If [x] and [y] are the concentration of dissociated and undissociated amino acid respectively.