Nutrition
15th Edition
ISBN: 9781337906371
Author: Sizer, Frances Sienkiewicz., WHITNEY, Ellie
Publisher: Cengage Learning,
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Question
Chapter 6, Problem 3SC
Summary Introduction
Introduction:
Proteins are complex macromolecules that are vital for the several different biological processes in the human body. Proteins are composed of amino acids, as building blocks or monomeric units. An amino acid has a carboxyl, an amino group, and an R group.
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What is the major difference between tertiary and quaternary protein structure?
The sequence of amino acids involved.
The involvement of R (radical) groups.
The number of polypeptides involved.
The side chain of arginine contains a—
hydroxyl group.
carboxyl group.
ether group.
aldehyde group.
guanidino group.
Attempt 8
Consider the hypothetical serine protease in the image,
which shows the specificity pockets. The S1 pocket has a
glutamic acid in the bottom, the S2 pocket is small and
R3
H.
R1
hydrophobic, and the S1' pocket is deep and hydrophobic.
Suggest a 3-amino acid sequence that this protease would
cleave and indicate between which sites the peptide bond
R
would be broken.
S2
Si
Which sequence would this protease cleave?
O Leu-Val-Arg
Arg-Val-Leu
Val-Leu-Arg
Val-Arg-Leu
Leu-Arg-Val
Arg-Leu-Val
W
Ma
tv
894
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, health-nutrition and related others by exploring similar questions and additional content below.Similar questions
- When a polypeptide is made, which of the following parts of the monomer are NOT part of the "backbone." Amino group R group Alpha carbon Carboxyl grouparrow_forwardThis image shows the tertiary structure of a protein segment. Tertiary structure results from different interactions, or forces, between groups. Move the example of each force to the appropriate description on the protein. Then, identify the major force controlling tertiary structure. (Need help) It says I'm wrong.arrow_forwardAffinity and specificity of protein-protein interactions are mainly mediated by many weak chemical bonds such as: Group of answer choices van der Waals forces hydrogen bonds hydrophobic interactions all of the abovearrow_forward
- The sequence of a peptide is given below. Ala-gly-val-leu-trp-lys-ser-phe-arg-proWhich peptide bond(s) are cleaved by chymotrypsin(arrow_forwardA polar functional group that forms disulfide bridges and stabilizes protein tertiary structure is O -NH2 O-COOH O -PO4 O-SH O -OHarrow_forwardAfter denaturation of a tertiary protein like lysozyme (with one polypeptide chain), the only remaining bonds between its monomer subunits will be: the disulfide bonds the van der Waals forces the peptide bonds the hydrogen bonds the ionic bondsarrow_forward
- Drag the correct amino acid into the corresponding box according to the roles they play. Reset Help Cycteine Proline Methionine First amino acid used in protein synthesis Forms kinks in the polypeptide forms disulfide bonds to stabilize backbone protein tertiary and quaternary structurearrow_forwardThe following shows a protein with mostly beta sheet secondary structures. Which force stabilizes the beta sheet secondary structure of proteins? hydrophobic interactions between nonpolar amino acid side chains within the protein. electrostatic interactions between lysine and aspartic acid residues within the protein. hydrogen bonding between hydrogen bond donors and hydrogen bond acceptors of the peptide backbone. covalent disulfide linkages between cysteine residues within the protein.arrow_forwardOptions are the same for the next slot.arrow_forward
- Drag each of the following items into the corresponding boxes to indicate the protein structural level that is predominantly affected by the chemical interactions listed. Some items may be placed in more than one box. Reset Help Hydrogen bonds between polar groups in amino acid side chains Hydrophobic interactions between amino acid side chains lonic bonds between positively- charged and negatively-charged amino acid side chains Peptide bonds Hydrogen bonds between carbonyl oxygens and amino nitrogens within a polypeptide backbone Disulfide bonds Primary structure Seconday structure Tertiary structure Quaternary structurearrow_forwardThe beta-pleated sheets are stabilized by hydrogen bonds among adjacent regions of the peptide backbone. True O Falsearrow_forwardUsing the DNA figure below to identify structures of the following letters: A= B= C= D= E= F: Circle a nucleotide for each backbone strand A B A G G A E Tarrow_forward
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