Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
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Chapter 18.6, Problem 18.20P
(a) What atoms are present in a planar unit in a protein chain?
(b) How many amino acid units do these atoms come from? Why are these units planar?
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Which of the following amino acids is most likely to be found on the outside of a soluble protein? Which is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acid side chain in each case and that the protein is folded up into its globularform.)(a) Leucine (b) Glutamate(c) Phenylalanine (d) Glutamine
Protein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct?
1) the folding pattern of a protein is ultimately determined by its amino acid sequence.
2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface.
3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains.
4) the overall folding pattern/shape of a protein molecule is termed its primary structure.
5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence.
More than one answer might be right
The amino acid valine has a nonpolar side chain, whereas serine has a polar side chain. Make a diagram of the two amino acids.(a) Why is the valine side chain nonpolar, yet the serine side chain is polar?(b) Which amino acid's side chains are hydrophilic and which are hydrophobic?
Chapter 18 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 18.2 - Prob. 18.1PCh. 18.2 - Prob. 18.2PCh. 18.3 - Prob. 18.3PCh. 18.3 - Examine the ball-and-stick model of valine in the...Ch. 18.3 - Indicate whether each of the following molecules...Ch. 18.3 - Prob. 18.6PCh. 18.3 - Prob. 18.7KCPCh. 18.3 - Prob. 18.8PCh. 18.3 - Prob. 18.9PCh. 18.3 - Prob. 18.10P
Ch. 18.3 - Prob. 18.11PCh. 18.3 - Prob. 18.12PCh. 18.4 - The proteins collagen, bovine insulin, and human...Ch. 18.4 - Prob. 18.2CIAPCh. 18.4 - Prob. 18.13PCh. 18.4 - Prob. 18.14PCh. 18.5 - Valine is an amino acid with a nonpolar side...Ch. 18.5 - Tripeptides are composed of three amino acids...Ch. 18.5 - Prob. 18.17PCh. 18.5 - Identify the amino acids in the following...Ch. 18.5 - Prob. 18.19PCh. 18.5 - Prob. 18.3CIAPCh. 18.5 - Prob. 18.4CIAPCh. 18.5 - Two of the most complete (balanced) proteins...Ch. 18.6 - Prob. 18.6CIAPCh. 18.6 - Prob. 18.7CIAPCh. 18.6 - (a)What atoms are present in a planar unit in a...Ch. 18.6 - Prob. 18.21PCh. 18.6 - Prob. 18.22PCh. 18.7 - Prob. 18.23PCh. 18.7 - Prob. 18.24PCh. 18.7 - Complete the following two sentences with either...Ch. 18.7 - Prob. 18.26KCPCh. 18.8 - Which of the following pairs of amino acids can...Ch. 18.8 - Look at Table 18.3 and identify the type of...Ch. 18.8 - In Figure 18.3, identify the amino acids that have...Ch. 18.8 - Prob. 18.30PCh. 18.9 - Prob. 18.31PCh. 18.10 - Another endoprotease is trypsin. Trypsin...Ch. 18.10 - Prob. 18.33PCh. 18.10 - Prob. 18.8CIAPCh. 18.10 - Prob. 18.9CIAPCh. 18 - Draw the structure of the following amino acids,...Ch. 18 - Prob. 18.35UKCCh. 18 - Prob. 18.36UKCCh. 18 - Prob. 18.37UKCCh. 18 - Prob. 18.38UKCCh. 18 - Threonine has two chiral centers. Draw L-threonine...Ch. 18 - Name four biological functions of proteins in the...Ch. 18 - Prob. 18.41APCh. 18 - Prob. 18.42APCh. 18 - Prob. 18.43APCh. 18 - Prob. 18.44APCh. 18 - Prob. 18.45APCh. 18 - Prob. 18.46APCh. 18 - Prob. 18.47APCh. 18 - Draw leucine and identify any chiral carbon atoms...Ch. 18 - Prob. 18.49APCh. 18 - Prob. 18.50APCh. 18 - Is histidine hydrophilic or hydrophobic? Explain...Ch. 18 - Prob. 18.52APCh. 18 - At neutral pH, which of the following amino acids...Ch. 18 - Prob. 18.54APCh. 18 - Prob. 18.55APCh. 18 - Prob. 18.56APCh. 18 - Prob. 18.57APCh. 18 - Proteins are usually least soluble in water at...Ch. 18 - Prob. 18.59APCh. 18 - Prob. 18.60APCh. 18 - Prob. 18.61APCh. 18 - Prob. 18.62APCh. 18 - Prob. 18.63APCh. 18 - (a)Identify the amino acids present in the peptide...Ch. 18 - Prob. 18.65APCh. 18 - Prob. 18.66APCh. 18 - Prob. 18.67APCh. 18 - Prob. 18.68APCh. 18 - Prob. 18.69APCh. 18 - Prob. 18.70APCh. 18 - Prob. 18.71APCh. 18 - Prob. 18.72APCh. 18 - Prob. 18.73APCh. 18 - Prob. 18.74APCh. 18 - Prob. 18.75APCh. 18 - What kind of bond would you expect between chains...Ch. 18 - Is the bond formed between each pair in Problem...Ch. 18 - Prob. 18.78APCh. 18 - Prob. 18.79APCh. 18 - Prob. 18.80APCh. 18 - Prob. 18.81APCh. 18 - Prob. 18.82APCh. 18 - Prob. 18.83APCh. 18 - Prob. 18.84APCh. 18 - Prob. 18.85APCh. 18 - Prob. 18.86APCh. 18 - Prob. 18.87APCh. 18 - Prob. 18.88APCh. 18 - Give an example of a protein that has quaternary...Ch. 18 - Prob. 18.90APCh. 18 - Prob. 18.91APCh. 18 - Prob. 18.92APCh. 18 - Prob. 18.93APCh. 18 - Prob. 18.94APCh. 18 - Prob. 18.95APCh. 18 - Prob. 18.96APCh. 18 - Prob. 18.97APCh. 18 - Prob. 18.98CPCh. 18 - Prob. 18.99CPCh. 18 - Prob. 18.100CPCh. 18 - Prob. 18.101CPCh. 18 - Prob. 18.102CPCh. 18 - Prob. 18.103CPCh. 18 - Prob. 18.104CPCh. 18 - Prob. 18.105CPCh. 18 - Prob. 18.106CPCh. 18 - Prob. 18.107CPCh. 18 - Prob. 18.108CPCh. 18 - Prob. 18.109GPCh. 18 - Prob. 18.110GPCh. 18 - Prob. 18.111GPCh. 18 - Prob. 18.112GP
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Which of the following amino acids is most likely to be found on the outside of a soluble protein, and which of them is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acidside chain in each case and that the protein is folded up into its globular form.)(a) Valine (b) Aspartate(c) Histidine (d) Alaninearrow_forwardWhat level of protein structure is determined by the following:(a) Peptide bonds between amino acids?(b) Hydrogen bonds between backbone carbonyl oxygen atoms and hydrogen atoms attached to backbone nitrogen atoms?(c) R group interactions that may involve Van der Waalsforces, ionic interactions, or hydrogen bonds?arrow_forwardWhat atoms are present in a planar unit in a protein chain?arrow_forward
- Consider a small protein containing 101 amino acid residues. The protein will have 200 bonds about which rotation can occur. Assume that three orientations are possible about each of these bonds. (a) Based on these assumptions, about how many random-coil con- formations will be possible for this protein? (b) The estimate obtained in (a) is surely too large. Give one reason why.arrow_forwardWhich of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (B) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (E) They require a high content of proline and glycinearrow_forwardWhich of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (8) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (€) They require a high content of proline and glycinearrow_forward
- Consider a small protein containing 101 amino acid residues. The proteinbackbone will have 200 bonds about which rotation can occur. Assume thatthree orientations are possible about each of these bonds.(a) Based on these assumptions, about how many random-coil conformationswill be possible for this protein?(b) The estimate obtained in (a) is surely too large. Give one reason why.arrow_forwardHow many different molecules composed of (a) two, (b) three, and (c) four amino acids, linked together by peptide bonds, can be made from the set of 20 naturally occurring amino acids?arrow_forwardIn Protein structure: a). Write the name of the four levels of protein structure, b). Explain the structural characteristics at each level,arrow_forward
- Currently, aspartic acid is forming an ionic interaction with arginine in a protein. Part a) If arginine is replaced with glutamic acid, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part b) If arginine is replaced with Lysine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction? Part c) If arginine is replaced with isoleucine, would the ionic interaction have its stability increased, decreased, or have no effect on the ionic interaction?arrow_forwardIf an oligosaccharide is attached to a protein via an O-glycosidic linkage which amino acid residue(s) are likely to be involved? O Glutamine O Serine O Histidine O Threonine O Both (b) and (d)arrow_forwardValine is an amino acid with a nonpolar side chain and serine is one with a polar side chain. Draw the two amino acids.(a) Why is the side chain for valine nonpolar, whereas the side chain for serineis polar?(b) Which amino acid has a hydrophilic side chain and which has a hydrophobic sidechain?arrow_forward
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