The interior core of globular proteins is typically composed of non-polar amino acid residues because of: a. beta-sheets b. hydrogen bonds c. the hydrophobic effect d. favourable electrostatic interactions
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- The interior core of globular proteins is typically composed of non-polar amino acid residues because of:
a. beta-sheets
b. hydrogen bonds
c. the hydrophobic effect
d. favourable electrostatic interactions
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- Which of the following bonding types is the most important in the nonaqueous interfaces between protein subunits? a. van der Waals interactions b. the hydrophobic effect c. ionic bonds d. disulfide bridgesWhich 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 roleWhich of the following describes the tertiary structure of proteins? A. Helices and sheets formed from hydrogen bonds between the amino acids of polypeptides B. The functional domains that form from interactions between different parts of the polypeptide C. The association of multiple polypeptides D. The linear sequence of amino acids making up the polypeptide
- Match the level of protein structure to its description: Primary Secondary Tertiary Quaternary A. Folding due to interactions among the peptide backbone B. Interactions among multiple polypeptide chains C. Sequence of amino acids D. Folding due to interactions among side chainsThe 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.Protein β-sheets are most likely to be found in: a either the interior or exterior of proteins, with no preference for one or the other. b the exterior of proteins, exposed to the aqueous environment. c the interior of proteins, away from the aqueous environment.
- What type of bonding is present in the primary structure of proteins? A. peptide bond B. hydrogen bond C. ionic bond D. more than one choice is correctWhich level(s) of protein structure result(s) from non-covalent interactions involving both backbone groups and side chains? (Select all that apply!) a) Primary b) Secondary c) Tertiary d) QuaternaryThe tertiary structure of many proteins reveals that nonpolar portions are primarily on the ________ of the molecule a. interior b. exterior
- A protein has a clearly defined hydrophobic core; however there is the residue glutamine within the hydrophobic core. How is this residue most likely stabilized (aka ‘made happy’) within this hydrophobic core? a. Hydrophobic interactions b. Interactions with a metal ion c. Hydrogen bonds d. Ionic interactions e. Electrostatic interactionsProtein secondary structure is stabilized by ... a) H-bonds between functional groups on amino acid side chains. b) interactions between hydrophobic amino acid R-groups. c) H-bonds between the N-H and C=O groups of the peptide backbone. d) a and c e) a, b and cPeptide bonding between amino acids in a polypeptide is an example of which type of chemical bonding? a) electrostatic b) covalent c) ionic d) hydrogen