Two amino acids are shown below. Name them in the blanks, and then draw the structure of the dipeptide they would form if a peptide bond connected them (in the order shown.) Draw the dipeptide as a Zwitterion, and name it in the blank. 118 H₂N-CH- CH3 + H₂N-CH₂-CⓇ
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- Which of the following characteristics is not common to carbohydrates, lipids, and proteins? a. They are composed of a carbon backbone with functionalgroups attached. b. Monomers of these molecules undergo dehydration synthesisto form polymers. c. Their polymers are broken apart by hydrolysis. d. The backbones of the polymers are primarily polar molecules. e. The molecules are held together by covalent bonding.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.7. Native conformation of proteins may result from: a) hydrophobic interactions b) H-bonds c) ionic bonds d) covalent bonds e) all a-d may contribute to native conformation
- 1)Explain 3 benefits of proteins forming higher oligomeric states. 2) Why are peptide bonds planar?1 which parts of amino acids are involved in tertiary structures ? 2 polar side chain can make hydrogen bonds. Draw any polar side chain and a hydrogen bond to water. 3 what are the functional group of the basic amino acids? 4 what is the organic functional group in a peptide bond? 5 Do all protein have quaternary structure? 6 phenylalanine and valine are non polar amino acids. Do you think they are more likely to be found on the exterior or interior of a protein1. Which of the following forms of lysine would you expect to predominate at low pH, neutral pH and high pH? 2. One of the 20 amino acids is unusual in that its side chain contains a ring that incorporates the amine functional group of the amino acid. What is the name of this amino acid? Write the chemical structure of this amino acid at physiological pH.
- 6.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 bond1. What biological molecule are required in the synthesis of protein( choose all that apply)? - phosphate ester - fatty acid (s) - alcohol - glycerol - amino acids 2. ATP is generated during A. Aldehyde reduction B. Alkene hydration C. Acetal synthesis D. Polysaccharide hydrolysis 3. What compound( biological classification) would be the result of protein complete hydrolysis in the mouth? A. Fatty acid and glycerol B. Monosaccharides C. Amino acids D. Disaccharide 4. The hydrophobic/ hydrophilic interaction are present in which protein structure level (s) (choose all that apply) ? - secondary - primary - tertiary -quaternary 5. Which protein structural level is/ are affected by the addition of an organic solvent isopropanol? A. Secondary B. Tertiary C. All are affected D. Quaternary1. Draw a circle around and give the name of each functional group in the following twomolecules. (Note: each line represents a covalent bond. If no atom is shown, assume there’s a carbon there.)
- 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 aboveWhich of these are considered “part” of each amino acid? A. Carboxyl acid group B. All of the options are correct C. R Group D. Amino group1.What reactive groups are involved in the formation of a peptide bond?2.A molecule of what substance must be removed in order to form a peptide bond?