Intramolecular ______ are responsible for formation of the most common three-dimensional shape in proteins, the alpha helix. a) van der waals forces b) hydrogen bonds c) covalent bonds d) ionic (electrostatic) interactions
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Intramolecular ______ are responsible for formation of the most common three-dimensional shape in proteins, the alpha helix.
a) van der waals forces
b) hydrogen bonds
c) covalent bonds
d) ionic (electrostatic) interactions
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- Which 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) Quaternarya) what does this suggest. b) suggest a macromolecule where this modification might occurWhat type of bonds/forces stabilize protein secondary structure? A) ionic (electrostatic) B) hydrogen bonds C) hydrophobic forces D) A and C O E) A, B and C
- Having peptides arranged in a beta sheet would be an example of a secondary structure A) True B) FalseWhich of the following features correctly describe aspects of protein structure? a) A protein possessing disulfide bonds will be more stable than a protein with the identical primary sequence lacking disulfide bonds. O b) B-sheets can only be formed from the anti-parallel arrangement of B-strands. c) Folding of a protein (tertiary structure) will typically result in a majority of the non-polar amino acids being distributed on the protein surface. d) both a and cWhich one of the following types of bond is principally responsible for holding the α-helix shape of a protein secondary structure : A) peptide B) disulfide C) hydrogen D)ionic
- Which of the following levels of protein structure can involve covalent bond formation? A) Primary B) Secondary C) Teritary D) Quaternary E) Primary and teritary F) Primary, teritary and quaternaryWhich of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…A coiled peptide chain held in place by hydrogen bonding between peptide bonds in the same chain is : A) Alpha helix B) Primary structure C) Tertiary structure E) Beta pleated sheets
- Lamin polypeptides (nuclear lamina) form dimers in which the central α-helical regions of two polypeptide chains are wound around each other. This is called a coiled coil. a) True b) FalseProteins have complex three-dimensional structures. These polymers are held into these specific shapes with a variety of intermolecular forces, covalent bonds, and ionic bonds. Alpha-helices and beta-sheets are examples of A) primary structure B) secondary structure C) tertiary structure D) quaternary structure10) Denaturation of a protein A) changes the primary structure of a protein. B) disrupts the secondary, tertiary, or quaternary structure of a protein. C) is always irreversible. D) hydrolyzes peptide bonds.