BCCB2000 Lecture 5 Questions Flashcards
(29 cards)
The ________ is the single shape a protein adopts under physiological conditions.
native conformation
Which statement is not true about the peptide bond? A. The peptide bond has partial double-bond character. B. The peptide bond is longer than the typical carbon-nitrogen bond. C. Rotation is restricted about the peptide bond. D. The carbonyl oxygen and the amide hydrogen are most often in a trans configuration with respect to one another.
B. The peptide bond is longer than the typical carbon-nitrogen bond.
The native structures of proteins are more stable than non-native conformations; they occupy a low-energy well when folded. True or False?
True
A polypeptide chain may have abrupt changes in direction and restriction in geometry because of the presence of: A. arginine B. glycine. C. proline D. leucine or isoleucine
C. proline
In an aqueous solution, protein conformation is determined by two major factors. One is the formation of the maximum number of hydrogen bonds. The other is the: A. formation of the maximum number of hydrophilic interactions. B. maximization of ionic interactions. C. minimization of entropy by the formation of a water solvent shell around the protein. D. placement of polar amino acid residues around the exterior of the protein. E. placement of hydrophobic amino acid residues within the interior of the protein.
E. placement of hydrophobic amino acid residues within the interior of the protein.
Nearly all peptide bonds are in the trans configuration because: A. cis peptide bonds are weaker. B. trans peptide bonds are stronger. C. cis peptide bonds prevent R groups from interacting. D. trans peptide bonds minimize steric hindrance of R groups.
D. trans peptide bonds minimize steric hindrance of R groups.
Most proteins contain an approximately equal amount of each of the standard amino acids. True or False?
False
Protein subunits in a multisubunit protein are held to each other primarily by: A. covalent bonds. B. hydrophobic interactions exclusively. C. both strong and weak interactions. D. hydrophobic and other weak interactions. E. All of the above
D. hydrophobic and other weak interactions.
An octapeptide composed of four repeating glycylalanyl units has: A. two free amino and two free carboxyl groups. B. a single free amino group on an alanyl residue. C. two free carboxyl groups, both on glycyl residues. D. a single free amino group on an alanyl residue and a single free carboxyl group on a glycyl residue. E. a single free amino group on a glycyl residue and a single free carboxyl group on an alanyl residue.
E. a single free amino group on a glycyl residue and a single free carboxyl group on an alanyl residue.
The reaction of two amino acids to form a dipeptide is a: A. cleavage. B. condensation. C. group transfer. D. oxidation-reduction. E. rearrangement.
B. condensation.
Which is true about the side chains of residues in an α-helix? A. They extend above or below the pleats. B. They extend radially outward from the helix axis. C. They point toward the center of the helix. D. They hydrogen bond extensively with each other
B. They extend radially outward from the helix axis.
In an alpha helix, the R groups on the amino acid residues: A. stack parallel within the interior of the helix. B. are mainly responsible for the hydrogen bonds that form the helix. C. extend radially outward from the helix axis. D. cause only right-handed helices to form. E. alternate between the outside and the inside of the helix.
C. extend radially outward from the helix axis.
Structural proteins that typically assemble into large cables or threads to provide mechanical support to cells or organisms are classified as ________ proteins.
Fibrous
The peptide alanylglutamylglycylalanylleucine has: A. five peptide bonds. B. no free carboxyl group. C. a disulfide bridge. D. four peptide bonds.. E. two free amino groups.
D. four peptide bonds.
Which one of the following statements is correct? A. beta bends often contain proline B. the alpha helix is stabilized primarily bu ionic interactions between the side chains of amino acids C. The alpha helix can be composed of more than one polypeptide chain. D. domains are a type of secondary structure E. beta sheets exist only in the antiparallel form
A. beta bends often contain proline
The subunits of a multisubunit proteins are always identical. True or False?
False
Which represents the backbone atoms of a protein? Note: R = amino acid side chain; N = nitrogen; Cα = alpha carbon; C = carbonyl carbon A. R1R2R3R4R5 B. repeating units of N-C C. repeating units of N-Cα-C D. repeating units of Cα-C
C. repeating units of N-Cα-C
Which of the following is correct with respect to the amino acid composition of proteins? A. Proteins contain at least one each of the twenty different standard amino acids. B. Proteins with different functions usually differ C. The average molecular weight of an amino acid in a protein increases with the size of the protein. D. Proteins with the same molecular weight have the same amino acid composition. E. Larger proteins have a more uniform distribution of amino acids than smaller proteins.
B. Proteins with different functions usually differ
The conformation of a protein enzyme determines whether it is functional or not. True or False?
True
The principle forces holding subunits of an oligomeric protein to each other are ________.
hydrophobic interactions
How many monomers are there in an oligomeric protein designated αβ2γ2?
αβ2γ2 = (1 x α) + (2 x β) + (2 x γ) = 5 monomers
Disulfide bridges can form in proteins ________.
between cysteine residues that are close in three-dimensional space, but not necessarily close in the primary structure
Removal of water from a chemical combination of particular monomers results in the formation of a polymer molecule. True or False?
True
Identify the CORRECT statement relating to the alpha helix in a protein: A. The alpha helix structure is maintained by hydrogen bonding between amino acids side chains B. The alpha helix makes up approximately the same percentage of most proteins C. The alpha helix is stabilized by hydrogen bonds between backbone amido groups and carbonyl groups of polypeptide chains D. The alpha helix includes all twenty amino acids at equal frequencies E. The alpha helix never contains proline
C. The alpha helix is stabilized by hydrogen bonds between backbone amido groups and carbonyl groups of polypeptide chains