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- Which bonds are planar (cannot rotate) in a polypeptide backbone? A. Ca-C bonds B. C-N bonds C. N-Cabonds D. Ca-Ca bondsDenaturation of a protein A. adds hydrogen bonds to the primary level of protein structure. B. breaks hydrogen bonds in the primary level of protein structure. C. adds hydrogen bonds to the secondary and tertiary levels of protein structure. D. breaks hydrogen bonds in the secondary and tertiary levels of protein structure.Which 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
- Three proteins K, L and M have the same % composition. Which is TRUE? A. The three proteins will have the same amino acid sequence B. The tertiary structure of these proteins will depend on the sequence of their amino acids C. The three proteins will have the same function D. The three proteins will have the same shapeWhich 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) QuaternaryCarbons is used in cells for a) forming the charge across the membrane by serving a positive cations b) as the structural backbone of most molecules c) forming the second most common element D) none of these
- One advantage of the protein structures solved by NMR comparing to the x-ray structures is: a. It can determine the absolute, unique structure. b. It can solve protein structures in solution, which might be more physiological relevant. c. It is much easier to solve the structure. d. It has higher resolution. e. It can solve proteins with higher molecular weight.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 is NOT TRUE about secondary structure in proteins? (More than one may apply) A. Stabilized by non-covalent bonds B. Is illustrated by DnaA molecules interacting in the ori C. Unravels at high temperatures when intramolecular non-covalent bonds are destroyed D. Occurs in a subregion of a protein E. Exemplified by beta sheets F. Describes the order of amino acids in a polypeptide
- The bonds that are important inthe secondary structure of a protein are a)hydrogen bonds b.peptide bonds c.hydrophobic interaction d.salt bridges e.disulfide bondsWhich of the following statements is incorrect about disulfide bonds? a. They form between two cysteine amino acids.b. They are noncovalent.c. They contribute to the tertiary structure of some proteins.d. They contribute to the quaternary structure of some proteins.e. They involve the loss of two hydrogen atoms.Which type of interaction stabilizes the alpha (α) helix and the beta (β) pleated sheet structures of proteins? Group of answer choices A. hydrophobic interactions B. peptide bonds C. hydrogen bonds D. nonpolar covalent bonds E. ionic bonds