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Concept explainers
(a)
Interpretation: The type of amino acid R group involved in hydrophobic interaction that contributes to tertiary protein structure has to be stated.
Concept introduction: The three-dimensional shape of the proteins obtained as a result of the interactions between the amino acid side chains is called the tertiary protein structure. The four types of attractive forces that give rise to tertiary proteins are: covalent disulphide bonds, electrostatic attractions, hydrogen bonds and hydrophobic attractions.
(b)
Interpretation: The type of amino acid R group involved in hydrogen bond that contributes to tertiary protein structure has to be stated.
Concept introduction: The three-dimensional shape of the proteins obtained as a result of the interactions between the amino acid side chains is called the tertiary protein structure. The four types of attractive forces that give rise to tertiary proteins are: covalent disulphide bonds, electrostatic attractions, hydrogen bonds and hydrophobic attractions.
(c)
Interpretation: The type of amino acid R group involved in disulphide bond that contributes to tertiary protein structure has to be stated.
Concept introduction: The three-dimensional shape of the proteins obtained as a result of the interactions between the amino acid side chains is called the tertiary protein structure. The four types of attractive forces that give rise to tertiary proteins are: covalent disulphide bonds, electrostatic attractions, hydrogen bonds and hydrophobic attractions.
(d)
Interpretation: The type of amino acid R group involved in electrostatic interaction that contributes to tertiary protein structure has to be stated.
Concept introduction: The three-dimensional shape of the proteins obtained as a result of the interactions between the amino acid side chains is called the tertiary protein structure. The four types of attractive forces that give rise to tertiary proteins are: covalent disulphide bonds, electrostatic attractions, hydrogen bonds and hydrophobic attractions.
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Chapter 20 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- Which of the following statement about quaternary structure of protein is correct? Select one: a. Quaternary structure is a force between different polypeptides. b. Hydrogen bond is an only force found in quaternary structure. c. Quaternary structure contains one polypeptide. d. Quaternary structure is an unfolded form of protein.arrow_forwardWhich of the following statement about proteins is correct a. alpha helix and Beta pleated sheets are considered quaternary structures b. a single polypeptide only has primary sytructure, secondary, tertiary, and quaternary structures require more than one polypeptide c. there are 30 essential amino acids that are the monomer building blocks of proteins d. polypeptides have a distinct polarity (directionality) with one end refered to as the free amino end, and the other called the free carboxyl endarrow_forwardWhich of the following statements are correct about protein structure (select all that apply)? A. Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein B. Only amino acids with a net charge may interact with other amino acids C. The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role. D. Hydrophobic interactions play a key role in protein folding E. Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acidsarrow_forward
- Using the amino acid phenylalanine, draw and specify the nature of each following tertiary structure interactions between:a. two cysteinesb. arginine and glutamic acidc. isoleucine and tyrosinearrow_forwardWhich of the following is not true about the properties of a peptide (amide) bond? a.The bond order of the peptide bond is 2 b.The bond is in resonance which makes it (and the 6 atoms around it and included within it) planar c.Delocalization of electrons through the peptide bond contributes to a net dipole for the bond d.Peptide bonds are very, very strongly favored to be in the trans conformation, but proline is an exception because it is more isoenergetic due to its sidechain ring, and can be cis.arrow_forwardWhich of the following are involved in protein secondary structure? select one or more : a. van der waal forces b. Disulfide bridges c. Hydrogen bonds d. Peptide bondsarrow_forward
- Which of the following is incorrect? (₁) a. A heterodimer is composed by two identical polypeptide chains b. The polypeptide chains in a multimeric protein are called subunits A homotrimer can be represented with the Greek letter alpha with a sub-index 3 d. Monomeric proteins do not have quaternary structure c.arrow_forwardWhich of the following statements is/are TRUE for globular proteins? A. sensitive to changes in pH & heat B. regular amino acid sequence C. soluble in water D. structural rolearrow_forwardThe tertiary structure of a protein is established by: a. The sequence of amino acids in the protein b. The molecular weight of the protein c. The total number of amino acids in the protein d. The number of disulfide bridges in the protein e. The net charge of the the protein at physioloical pH.arrow_forward
- Indicate which of the following are present in the primary, secondary, tertiary, and quaternary structures ofproteins: a. peptidebonds b. hydrogen bonds between adjacentpeptides c. hydrogen bonds within a singlepeptide d. hydrophobic interactions e. association of four polypeptide chainsarrow_forwardDraw the chemical structure of an alanine pentapeptide. Indicate the location of each peptide bond. Label the phi () and psi () dihedral angles. Name and briefly define the four levels of protein structure.arrow_forwardHydrogen bonds and hydrophobic interactions play important roles in stabilizing and organizing biological macromolecules. Describe how hydrogen bonds and hydrophobic interactions affect the form and function of proteins.arrow_forward
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