Nutrition
15th Edition
ISBN: 9781337906371
Author: Sizer, Frances Sienkiewicz., WHITNEY, Ellie
Publisher: Cengage Learning,
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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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True or False: Protein primary structure results from covalent bonding between side chains, e.g. disulfide bonds.
True
False
Hydrophobic interactions associated with protein tertiary structure involves:
Acidic and basic amino acid side chains
All of the above
Nonpolar amino acid side chains
Hydrogen bonding between polar amino acid side chains
Affinity 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 above
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- Which of the which of the following forces are involved in maintaining the primary structure of a protein? covalent bonds hydrogen bonds ionic interactions hydrophobic interactionsarrow_forwardWhich of the following statements concerning complete protein hydrolysis is incorrect? Primary structures are preserved Tertiary and secondary structures are disrupted All peptide bonds are broken Water is a reactant in the processarrow_forwardAmino acids attached together in a straight line structure, is called: Primary structure Quaternary structure Secondary structure Tertiary structurearrow_forward
- Which of the following enzymes creates a covalent bond that links amino acids in a polypeptide? Protein disulfide isomerase Hsp70 Peptidyl-prolyl isomerase Calreticulinarrow_forwardLabel: 1) the type of chemical bonds between the amino acids (e.g. covalent bond, ionic bond, metallic bond) 2) the type of interparticle forces of attraction occurring within the protein and with its environment *Indicate at least four observed interparticle forces of attraction *pink - negatively charged, blue - positively charged, yellow - nonpolar and uncharged, green - polar and uncharged *[See example picture] The chemical bond (shown by the arrow) is depicted as a line between the amino acids. Interparticle forces of attraction, such as the one between Phe and Glu (boxed), are not represented by lines but rather by the proximity of amino acids.arrow_forwardDefinition of Proteins What is the Formation / Synthesis and breakdown: Amino acids Amino group, carboxyl group, R-group/ side chain/body/core Deaminationarrow_forward
- the linear sequence of amino acids in a polypeptide chain is referred to as a proteins _________ structure primary secondary tertiary quaternaryarrow_forwardThe primary structure of a protein describes Number of peptide linkages Sequence of the amino acid Number of amino acid present Type of linkage in the amino acid backbonearrow_forwardThe specific amino acid sequence of a protein and the resulting hydrogen bond is its ___ - primary structure - secondary structure - tertiary structure - quatemary structurearrow_forward
- A peptide bond... is a version of an ester bond is a version of an amide bond is the basis of protein secondary structure is formed by addition of waterarrow_forwardAdjacent nucleotides in an RNA chain are held together by: All of these choices are correct. the hydrophobic effect. hydrogen bonding. covalent bonding. ionic bonding.arrow_forwardWhich statement about quaternary structure is TRUE? Quaternary structure is unaffected by acids or heat. Quaternary structure is determined by the same interaction that holds an α-helix together. Quaternary structure is how prosthetic groups are held in a protein. Quaternary structure is the position of subunits in the overall structure of a protein. All proteins have quaternary structurearrow_forward
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