Which statement best describes the protein structure shown below?
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- Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary and secondary (b) primary and tertiary (c) secondary, tertiary, and quaternary (d) primary, secondary, and tertiary (e) primary, secondary, tertiary, and quaternaryWhich of the following statement is not true? In a secondary structure the consecutive residues have phi and psi values that are quite different. The Ramachandran diagram defines the restrictions of polypeptide backbone conformation. Two α helices with hydrophobic side chains repeated in a regular pattern can form dimeric structures in water. Greek key motifs occur frequently in antiparallel β structures. Both α helices and β sheets can be amphipathic.In the following diagram of a portion of a protein, label the types of interactions that are shown. What level of protein structure are these interactions producing?
- Which of the following statements best describes the hydrophobic character of bacteriorhodopsin (2BRD)? Both the interior and exterior of the protein are hydrophobic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, but the central core of the trimer is hydrophobic. Both the interior and exterior of the protein are hydrophobic, but the central core of the trimer is hydrophilic.Which of the following statements are true? The local folding of the polypeptide in some regions gives rise to the secondary structure of the protein. The most common secondary structures are the α-helix and β-pleated sheet structures. Certain amino acids have a propensity to form an α-helix, while others have a propensity to form a β-pleated sheet. Select the correct answer below: 1 and 2 1 and 3 2 and 3 all of the aboveWhat does the "alpha" indicate in "α-helix"? It is a Greek helix. It's position lies above the beta-pleated-sheet. It has only the one enantiomer. It predominates in the 3º structure of the protein. None of these.
- The structure shown below belongs to which family of protein tertiary structure? PDB: 1Z4A 1) a/ß barrel 2) B-barrel 3) a-helix bundle 4) aß-sandwichThe different types of interactions that stabilize the protein tertiary structure are illustrated in the diagram below. Which type of interaction moves some part of the polypeptide chain toward the inside of the folded protein? OH Hydrophilic OH CH₂ interaction with water Hydrogen bond -NH₂3-0- C Salt bridge -CH₂-OH C=0 H-N H 0-CH,- I H Hydrogen bond Salt bridge O Disulfide bond 222 -SIS Hydrophobic interaction 200 O Hydrogen bond O Hydrophilic interaction Disulfide bonds B-Pleated sheet O Hydrophobic interaction CH₂ CH₂ a Helix CH3 CH3 Hydrogen bondsWhat general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
- Consider beta-sheet comprised of twelve amino acid residues (two strands of six residues each). How many hydrogen bonds should be formed between backbone atoms in this sheet?Refer to the figure below. Replacing lysine with another amino acid in the protein may alter the shape and function of the protein. Replacing lysine with which type(s) of amino acid(s) would lead to the least amount of change in the tertiary structure of this protein? Explain.Why is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.
