Podcast
Questions and Answers
What is the role of annular lipids in membrane proteins?
What is the role of annular lipids in membrane proteins?
- Encapsulate the protein in a water layer
- Enhance protein flexibility in the membrane
- Repel proteins from the membrane surface
- Form a bilayer shell around the protein (correct)
Which amino acid residues are commonly found at the interface between lipid and water in transmembrane proteins?
Which amino acid residues are commonly found at the interface between lipid and water in transmembrane proteins?
- Cysteine and Serine
- Alanine and Glycine
- Tyrosine (Tyr) and Tryptophan (Trp) (correct)
- Phenylalanine (Phe) and Methionine (Met)
How do proteins with a narrow hydrophobic band influence lipids in the membrane?
How do proteins with a narrow hydrophobic band influence lipids in the membrane?
- Promote lipid bilayer formation around the protein
- Enhance lipid-protein interactions
- Encourage lipids to take on less extended conformations (correct)
- Repel lipids from the protein surface
What is the main function of charged residues like Arginine (Arg) and Lysine (Lys) in membrane proteins?
What is the main function of charged residues like Arginine (Arg) and Lysine (Lys) in membrane proteins?
Which of the following characteristics apply to α-helical proteins in membrane-spanning segments?
Which of the following characteristics apply to α-helical proteins in membrane-spanning segments?
What type of irregularities are commonly observed in helices of multi-spanning membrane proteins?
What type of irregularities are commonly observed in helices of multi-spanning membrane proteins?
What kind of residues are favored in the interfacial region of the membrane-spanning helix?
What kind of residues are favored in the interfacial region of the membrane-spanning helix?
Why is tilting the helix problematic in spanning a biological membrane?
Why is tilting the helix problematic in spanning a biological membrane?
What role does the C-terminal end of the helix play in a bacterial K+ channel?
What role does the C-terminal end of the helix play in a bacterial K+ channel?
Which type of proteins are especially abundant and have 4, 7, or 12 transmembrane segments?
Which type of proteins are especially abundant and have 4, 7, or 12 transmembrane segments?
What kind of residues predominantly make up the central region of multi-spanning trans-membrane proteins?
What kind of residues predominantly make up the central region of multi-spanning trans-membrane proteins?
Which residue type is tolerated in small numbers in the section of the helix traversing the membrane?
Which residue type is tolerated in small numbers in the section of the helix traversing the membrane?
What is the most abundant group of residues in transmembrane helices?
What is the most abundant group of residues in transmembrane helices?
Which type of residues are rare in transmembrane helices?
Which type of residues are rare in transmembrane helices?
What kind of amino acids are often present in transmembrane domains involved in transport, ligand binding, and catalysis?
What kind of amino acids are often present in transmembrane domains involved in transport, ligand binding, and catalysis?
How do hydrophilic side chains in transmembrane domains interact with the lipid bilayer?
How do hydrophilic side chains in transmembrane domains interact with the lipid bilayer?
In the structure of the glucose transporter, what lines the hydrophilic transmembrane pore?
In the structure of the glucose transporter, what lines the hydrophilic transmembrane pore?
What stabilizes the structure of membrane proteins by interacting with the lipid bilayer?
What stabilizes the structure of membrane proteins by interacting with the lipid bilayer?
