Concept explainers
(a)
Interpretation:
Following amino acids are on the surface of a globular protein or fibrous protein has to be identified.
Concept introduction:
- Fibrous protein is a tough, insoluble protein whose protein chains form fibers or sheets.
- Globular protein is a water soluble protein whose chain is folded in a compact shape with hydrophilic groups on outside.
(b)
Interpretation:
Following amino acids are on the surface of a globular or fibrous protein has to be identified.
Concept introduction:
- Fibrous protein is a tough, insoluble protein whose protein chains form fibers or sheets.
- Globular protein is a water soluble protein whose chain is folded in a compact shape with hydrophilic groups on outside.
(c)
Interpretation:
Following amino acids are on the surface of a globular or fibrous protein has to be identified.
Concept introduction:
- Fibrous protein is a tough, insoluble protein whose protein chains form fibers or sheets.
- Globular protein is a water soluble protein whose chain is folded in a compact shape with hydrophilic groups on outside.
(d)
Interpretation:
Following amino acids are on the surface of a globular or fibrous protein has to be identified.
Concept introduction:
- Fibrous protein is a tough, insoluble protein whose protein chains form fibers or sheets.
- Globular protein is a water soluble protein whose chain is folded in a compact shape with hydrophilic groups on outside.
(e)
Interpretation:
Following amino acids are on the surface of a globular or fibrous protein has to be identified.
Concept introduction:
- Fibrous protein is a tough, insoluble protein whose protein chains form fibers or sheets.
- Globular protein is a water soluble protein whose chain is folded in a compact shape with hydrophilic groups on outside.
(f)
Interpretation:
Following amino acids are on the surface of a globular or fibrous protein has to be identified.
Concept introduction:
- Fibrous protein is a tough, insoluble protein whose protein chains form fibers or sheets.
- Globular protein is a water soluble protein whose chain is folded in a compact shape with hydrophilic groups on outside.
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Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
- Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.arrow_forwardAt neutral pH, which of the following amino acids has a net positive charge, which has a net negative charge, and which is neutral? (Hint: Draw the various charged forms of each amino acid before deciding.)(a) Aspartic acid (b) Histidine (c) Valinearrow_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_forward
- In each of the following pairs of amino acids, identify which amino acid would be more soluble in water: (a) Ala, Leu; (b) Tyr, Phe; (c) Ser, Ala; (d) Trp, Hisarrow_forwardThe 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?arrow_forwardOur understanding of how proteins fold allows us to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence :a)Where might bends or βturns occur? b)Where might intrachain disulphide cross-linkages be formed? c)Assuming that this sequence is part of a bigger globular protein, indicate the probable location (on the surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln and Lys. Explain your reasoningarrow_forward
- If 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_forwardTripeptides are composed of three amino acids linked by peptide bonds. Given a set of amino acids, you can make several different tripeptides.(a) Use the three-letter shorthand notations to name all the tripeptides that can be made from serine, tyrosine, and glycine. Each amino acid will be used once in each tripeptide.(b) Draw the complete structure of the tripeptides that have glycine as the N-terminal amino acid.arrow_forwardIn the peptide Ala – Gly – Val – Phe – Tyr, a carboxylate (-COO-) group would bound in which amino acid? A) Gly b) Ala c) Phe d) Tyr Which amino acid forms disulfide bonds? A) Met b) Cys c) Arg d) Pro The sequence Gly-Pro-Pro is often found in collagen. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structurearrow_forward
- (a) Draw the structure of the two possible dipeptides that can be formed by combining glycine and asparagine. (b) In each dipeptide, label the N- and C-terminal amino acids. (c) Name each peptide using three-letter symbols.arrow_forwardConsider 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_forwardCurrently, 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_forward
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