Question 1
The protein in the diagram is (circle all that apply):
Group of answer choices
a) a peripheral membrane protein
b) an integral membrane protein
c) a lipid anchored protein
Question 2
The protein shown in the diagram could potentially function as (circle all that apply):
Group of answer choices
a) a receptor
b) a transmembrane anchor
c) a pore or channel
Question 3
The protein shown in the diagram has which of the following (choose all that apply)?
Group of answer choices
a) primary structure
b) secondary structure
c) tertiary structure
d) quaternary structure
Question 4
The structures in the red circles represent which of the following (choose all that apply)?
Group of answer choices
a) fatty acid
b) cholesterol
c) oligosaccharides
d) GPI anchors
Question 5
The structures in the red squares represent which of the following (choose all that apply)?
Group of answer choices
a) fatty acids
b) cholesterol
c) oligosaccharides
d) GPI anchors
Question 6
The red arrow is pointing to which of the following (choose all that apply)?
Group of answer choices
a) an intramolecular bond
b) an intermolecular bond
c) an amino acid
d) a disulfide bond
e) a van der Waals interaction
Question 7
Which of the following are important for stabilizing the tertiary structure of this protein (circle all that apply)?
Group of answer choices
a) the structure in the red squares
b) the structure in the red circles
c) the structure indicated by the red arrow
d) hydrophobic/hydrophilic interactions
e) hydrogen bonding
f) van der Waals interactions
Question 8
What structural feature allows this protein to span the lipid bilayer?
Group of answer choices
a) quaternary structure
b) beta pleated sheets
c) alpha helices
d) both beta pleated sheets and alpha helices
Question 9
What chemical bonding or interaction stabilizes the structure you chose for “8”?
Group of answer choices
a) ionic bonds
b) van der Waals interactions
c) hydrogen bonding
d) covalent bonding
e) hydrophobic/hydrophilic interactions
Question 10
You entered the primary amino acid sequences of this protein into the protein database and generated one of the plots shown below in which the relative average hydrophobicity of amino acids is plotted on a scale of 1-10 (with 1 being very hydrophilic and 10 being very hydrophobic). The individual data points on the graph represent the average hydrophobicity of 5 amino acid blocks (for example, amino acids 1-5, 2-6, 3-7, etc), all the way along the protein.
Which of the graphs below (A-F) describes the protein in the diagram at the beginning of the problem set?
1. The protein in the diagram is an integral membrane protein.
2. The protein shown in the diagram could potentially function as a receptor.
3. the protein shown in the diagram has quaternary structure.
4. The structure in the red circle represents cholesterol.
Question 1 The protein in the diagram is (circle all that apply): Group of answer choices...
1. Which of the following statements is consistent with the structural motifs in 1OPF? This protein has tertiary structure, where each subunit is a large parallel beta barrel. This protein has quaternary structure, where each subunit is a large antiparallel beta barrel. This protein has tertiary structure, where each subunit is a large antiparallel beta barrel. This protein has quaternary structure, where each subunit is a large parallel beta barrel. 3. Given the information in the PDB entry for 1OPF,...
Explain why α-helices are most commonly observed in transmembrane protein sequences when the distance from one side of a membrane to the other can be spanned by significantly fewer amino acids in a β-strand conformation. Match the items in the left column to the appropriate blanks in the sentences on the right. prevents within a The structure of an a-helix promotes stretch of amino acids, and at the same time contiguous interactions with other important molecules involved in in the...
Explain why α-helices are most commonly observed in transmembrane protein sequences when the distance from one side of a membrane to the other can be spanned by significantly fewer amino acids in a β-strand conformation. Match the items in the left column to the appropriate blanks in the sentences on the right. noncontiguous The structure of an a-helix promotes within a stretch of amino acids, contiguous and at the same time interactions with other important molecules involved in in the...
O points 1 attempts left Check my work What interactions are responsible for maintaining quaternary protein structure? Select all that apply O ionic bridges van der Waals forces hydrogen bonding O disulfide bonds peptide bonds
Which of the following forces affect protein conformation: (May be more than one answer) a.)Hydrogen Bonds b.)Electrostatic attractions c.)Van der Waals interactions d.)Hydrophobic effect e.)Covalent Bonds
QUESTION 1 A segment of a protein has a large positive hydropathic index. This segment of the protein is O A. hydrophobic and found on the outside of the protein B. hydrophilic and buried in the hydrophobic core of the protein ochydrophobic and most likely found buried inside the protein O D. hydrophilic and found on the outside of the protein QUESTION 2 The tertiary structure of a protein is the result of which of the following type(s) of interactions...
24. The _______ of amino acids in a protein is referred to as its primary structure. A) twisting B) sequencing C) folding D) none of these 25. The structure of a protein is most important because the _______ of the amino acids determines its overall shape, function and properties. A) primary, twisting B) primary, sequencing C) secondary, twisting D) secondary, folding E) none of these 26. The secondary structure of a protein is due to_______ between amino acid residues. A) hydrophobic interactions B) hydrogen bonding...
- DELIS SUSTESTD comprennen n eu Question Completion Status QUESTION 1 A segment of a protein has a large positive role index. This segment of the protein is O A hydrophobic and found on the outside of the protein OB. hydrophilic and buried in the hydrophobic core of the protein O Chydrophobic and most likely found buried inside the protein O D. hydrophilic and found on the outside of the protein QUESTION 2 The tertiary structure of a protein is...
How are lipid bilayers formed? What is their fluidity dependent on? Group of answer choices: - Hydrophobic interactions are the driving force of forming bimolecular sheets of lipids spontaneously. Due to the hydrophobic effect, any tears in the lipid bilayer cause it to spontaneously rearrange to eliminate the free edge. Membrane fluidity depends on the percentage of unsaturated fatty acids. - Hydrophobic interactions are the driving force of forming bimolecular sheets of lipids spontaneously. Due to the hydrophobic effect, any...
Which of the following is true of secondary structure in protein folding? Pick ALL that apply. A. It involves hydrogen bonding. B. It involves the side chains. C. It involves hydrophobic interactions. D. It results in alpha helicies with the side chains hidden inside the helix. E. It results in beta-pleated sheets with side chains sticking out of the plain of the sheet. F. It involves the peptide backbone.