Connect 1-Semester Online Access for Principles of General, Organic & Biochemistry
2nd Edition
ISBN: 9780077633707
Author: Janice Smith
Publisher: Mcgraw-hill Higher Education (us)
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Chapter 16.3, Problem 16.6P
Identify the amino acid shown with all uncharged atoms in the ball-and-stick model, and draw the neutral, positively charged, and negatively charged forms of the amino acid.
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Identify the amino acid shown with all uncharged atoms in the ball-and-stick model, and draw the neutral, positively charged, and negatively charged forms of the amino acid.
What does the "alpha" indicate in "α-amino acid"?
That the -COOH group is below the plane of the ring.
That the amino group is the first group in the compound.
That the alpha-carbon has a -NH2 attached.
The the amino acid is the dominant form.
As we’ve discussed, a peptide bond is made when amino group of one amino acid combines with the carboxylic acid group of another amino acid (releasing a water molecule in the process). The C-N bond formed in this process is called a peptide bond. Peptide bonds have a few properties that might be unexpected.
b) Another observation is that although the N-H of the peptide bond is able to serve as a H-bond donor the N atom of the peptide bond does not serve as an effective H-bond acceptor. Provide an explanation for this observation, using Lewis structures, VSEPR theory and/or valence bond theory as appropriate.c) It is also fairly accepted that while proteins undergo dynamic motions and conformational changes, and while R groups can freely rotate about Cα, it is generally not possible to freely rotate around a peptide bond. Please explain this observation, using a picture showing relevant orbitals on relevant atoms (your answer for part (a) might provide a useful basis for your reasoning…
Chapter 16 Solutions
Connect 1-Semester Online Access for Principles of General, Organic & Biochemistry
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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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- What special role does the amino acid cysteine have in the peptides vasopressin and oxytocin?arrow_forwardFor the tripeptide GlyAlaCys a. What amino acid is located at the peptides N-terminal end? b. What amino acid is located at the peptides C-terminal end? c. How many peptide bonds are present? d. How many amide linkages are present?arrow_forwardDraw a segment of the backbone of a protein that is long enough for three peptide linkages to be present.arrow_forward
- To which family of mirror-image isomers do nearly all naturally occurring amino acids belong?arrow_forwardFor the tripeptide SerArgIle which amino acid residues a. are hydrophilic b. are hydrophobic c. possess polar neutral R groups d. participate in two amide linkagesarrow_forwardIdentifying Amino Acids Which of the following molecules is an amino acid?arrow_forward
- (a) How many tripeptides can be made from glycine, alanine, and leucine, using each amino acid only once per tripeptide? (b) Write the structural formulas of these tripeptides and name them in the shorthand abbreviation used for showing amino acid sequences.arrow_forwardWhat characteristics indicate that amino acids exist as zwitterions?arrow_forwardFill in the blanks in the following statements: aThe order of the amino acids in a protein is the ______ structure of that protein. The _______ of the backbone chain of a protein is the secondary structure of that protein. The tertiary structure of a protein describes the ______ of the secondary structure. b Hydrogen bonding between the oxygen atoms of carbonyl groups and the hydrogen atoms of amide groups in the same protein chain gives the secondary structure, called the ______. c Hydrogen bonding between the oxygen atoms of carbonyl groups and the hydrogen atoms of amide groups in the adjacent protein chain gives the secondary structure, called the ______.arrow_forward
- On complete hydrolysis, a polypeptide gives two alanine, one leucine, one methionine, one phenylalanine, and one valine residue. Partial hydrolysis gives the following fragments: Ala-Phe, Leu-Met, Val-Ala, Phe-Leu. It is known that the first amino acid in the sequence is valine and the last one is methionine. What is the complete sequence of amino acids?arrow_forwardIdentify the R group of the side chain in the following amino acids that results in the side-chain classification indicated in parentheses see Table 19.1: a. tyrosine neutral, polar b. glutamate acidic, polar c. methionine neutral, nonpolar d. histidine basic, polar e. cysteine neutral, polar f. valine neutral, nonpolararrow_forwardIn naming an amino acid, how may one indicate whether it is in the D or L configuration? Support answer with illustration. How are amino acids linked together in a protein molecule? Write the general structure of the tripeptide lys-phe-meth. Show their peptide bonds What is protein denaturation? Give 5 agents that can denature proteins. Is it possible for a denatured protein to revert back into its native/ original form? Explain your answer.arrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY