Principles of General, Organic, Biological Chemistry
2nd Edition
ISBN: 9780073511191
Author: Janice Gorzynski Smith Dr.
Publisher: McGraw-Hill Education
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Textbook Question
Chapter 16.2, Problem 16.2P
How do the OH groups in Ser, Thr, and Tyr differ?
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Chapter 16 Solutions
Principles of General, Organic, Biological Chemistry
Ch. 16.2 - In addition to the amino and carboxyl groups, what...Ch. 16.2 - How do the OH groups in Ser, Thr, and Tyr differ?Ch. 16.2 - Draw both enantiomers of each amino acid in...Ch. 16.2 - Which of the following amino acids is naturally...Ch. 16.3 - Draw the structure of the amino acid valine at...Ch. 16.3 - Identify the amino acid shown with all uncharged...Ch. 16.3 - Draw the positively charged, neutral, and...Ch. 16.4 - Identify the N-terminal and C-terminal amino acid...Ch. 16.4 - (a) Identify the N-terminal amino acid in the...Ch. 16.4 - Identify the individual amino acids in each...
Ch. 16.4 - Prob. 16.11PCh. 16.5 - Prob. 16.12PCh. 16.6 - Prob. 16.13PCh. 16.6 - Draw the structures of each pair of amino acids...Ch. 16.6 - The fibroin proteins found in silk fibers consist...Ch. 16.7 - Prob. 16.16PCh. 16.7 - Prob. 16.17PCh. 16.8 - Prob. 16.18PCh. 16.8 - Prob. 16.19PCh. 16.8 - Prob. 16.20PCh. 16.9 - Prob. 16.21PCh. 16.9 - Prob. 16.22PCh. 16.9 - The nerve gas sarin acts as a poison by covalently...Ch. 16.10 - Prob. 16.24PCh. 16 - Prob. 16.25UKCCh. 16 - Prob. 16.26UKCCh. 16 - For each amino acid: [1] draw the L enantiomer in...Ch. 16 - For each amino acid: [1] give the name; [2] give...Ch. 16 - For the given tripeptide: (a) identify the amino...Ch. 16 - For the given tripeptide: (a) identify the amino...Ch. 16 - Label the regions of secondary structure in the...Ch. 16 - Label the regions of secondary structure in the...Ch. 16 - What type of interactions occur at each of the...Ch. 16 - Using the given representations for an enzyme and...Ch. 16 - Naturally occurring amino acids are L--amino...Ch. 16 - Why do neutral amino acids exist as zwitterions...Ch. 16 - The amino acid alanine is a solid at room...Ch. 16 - Why is phenylalanine water soluble but...Ch. 16 - Draw the structure of a naturally occurring amino...Ch. 16 - Draw the structure of a naturally occurring amino...Ch. 16 - For each amino acid: [1] draw the l enantiomer in...Ch. 16 - For each amino acid: [1] draw the l enantiomer in...Ch. 16 - Draw both enantiomers of each amino acid and label...Ch. 16 - Which of the following Fischer projections...Ch. 16 - For each amino acid: [1] give the name; [2] give...Ch. 16 - For each amino acid: [1] give the name; [2] give...Ch. 16 - Draw the amino acid leucine at each pH: (a) 6; (b)...Ch. 16 - Draw the amino acid isoleucine at each pH: (a) 6;...Ch. 16 - Draw the structure of the neutral, positively...Ch. 16 - Draw the structure of the neutral, positively...Ch. 16 - For each tripeptide: [1] identify the N-terminal...Ch. 16 - For each tripeptide: [1] identify the N-terminal...Ch. 16 - For the given tripeptide: (a) identify the amino...Ch. 16 - For the given tripeptide: (a) identify the amino...Ch. 16 - Locate the peptide bond in the dipeptide shown in...Ch. 16 - Label the N-terminal and C-terminal amino acids in...Ch. 16 - Draw the structures of the amino acids formed when...Ch. 16 - Draw the structures of the amino acids formed when...Ch. 16 - What amino acids are formed by hydrolysis of the...Ch. 16 - Give the three-letter abbreviations for the amino...Ch. 16 - What is the difference between the primary and...Ch. 16 - What is the difference between the tertiary and...Ch. 16 - What type of intermolecular forces exist between...Ch. 16 - Which of the following pairs of amino acids can...Ch. 16 - List two amino acids that would probably be...Ch. 16 - List two amino acids that would probably be...Ch. 16 - Compare -keratin and hemoglobin with regards to...Ch. 16 - Compare collagen and myoglobin with regards to...Ch. 16 - When a protein is denatured, how is its primary,...Ch. 16 - Hydrogen bonding stabilizes both the secondary and...Ch. 16 - Describe the function or biological activity of...Ch. 16 - Describe the function or biological activity of...Ch. 16 - Use the given representations for an enzyme,...Ch. 16 - Use the given representations for an enzyme and...Ch. 16 - How are enzyme inhibitors used to treat high blood...Ch. 16 - How are enzyme inhibitors used to treat HIV? Give...Ch. 16 - What structural feature in -keratin makes...Ch. 16 - Why does the -keratin in hair contain many...Ch. 16 - Why must vegetarian diets be carefully balanced?Ch. 16 - Why does cooking meat make it easier to digest?Ch. 16 - Sometimes an incision is cauterized (burned) to...Ch. 16 - Prob. 16.82APCh. 16 - How is sickle cell disease related to hemoglobin...Ch. 16 - The silk produced by a silkworm is a protein with...Ch. 16 - Explain the difference in the mechanism of action...Ch. 16 - How are blood enzyme levels used to diagnose...Ch. 16 - Explain why two amino acids aspartic acid and...Ch. 16 - Prob. 16.88CP
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- 2. Draw the tripeptide containing Ser-Ala-Val.arrow_forward43. Specify expressions specific to panaxosides. I. taken from ginseng II. there are glucose and arabinose monosaccharides in this compound III. taken from Japanese angelica-tree IV. tetratcyclic triterpen saponins V. spirostanol type glycoside VI. dimer structure VII. biglycosides VIII. dammaran group IX. differ for number of hydroxyl groups X. furostanol type glycoside A) II; VI; VII; IX; X B) III; V; VIII C) I; IV; VIII; IX D) I; VIII; IX E) I; III; V; VII; VIII; Xarrow_forwardWhat is the structure of SeF5NF2?arrow_forward
- Do the amino acid sequences: valine-asparagine and asparagine-valine represent the same compound? Explain.arrow_forward. How many unique amino acid sequences are possible for a tripeptide containing only the amino acids gly, ala, and cys, with each amino acid occurring only once in each molecule?arrow_forward22-59 What is the effect of salt bridges on the tertiary structure of proteins?arrow_forward
- 8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) • Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at pH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated ammonium sulfate? Explain your answer. 5 83°F Cloudyarrow_forwardBUILDING BLOCKS MONOSACCHARIDE AMINO ACIDS FATS AND OILS NUCLEOTIDE Cell wall Protein complex Membrane 2. Cellulose Protein sub-unit Phospholipid Saccharide 1 Fatty acid GROUPS Monosaccharide/ Disaccharide/ Dipeptide/ Simple Lipid/ DNA / RNA 3. Oligopeptide/ Compound Lipid/ Polysaccharide Polypeptide/ Proteins 4. COMPOSITION С, Н, О C, H, O, N, P C, H, O (fewer Oxygen than CarbonC, H, O, P 5.L 6. BOND / LINKAGE 7. Peptide bond Ester Bond 8. Cushions your internal organs Structural, Storage, Transport, Receptor, Contractile, Defensive, against trauma. Forms the Hormonal, Sensory, 9. Stores information that is used to make proteins. MAIN FUNCTION structure of cell membranes MAIN TEST INDICATION Molisch test 10. Emulsion Test/ Dische Diphenylamine Test / Amplification Test Solubility test/ Sudan Stain Test REAGENT Benedict's/ lodineSoln NaOH +CusO4 11. SYBR Green Dye DIGESTION TAKES PLACE 12. Stomach 13. 14. at SICKNESS/ 15. Sickle cell anemia arteriosclerosis Genetic disease DISEASEarrow_forward
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