Why are beta sheets so commonly found in transmembrane proteins?
Answer: They only require 9-11 residues to traverse the lipid bilayer (as opposed to 21-25 when traversing with an alpha helix). Therefore a given amount of genetic material can make more transmembrane proteins when they are in a beta sheet configuration.
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Membranes and Membrane Transport
- T/F, the two monolayers have different lipid and protein composition
- T/F, Membranes are symmetric, homogeneous structures
- Which terminal are Glycosyl Phosphatidylinositol proteins always bound to?
- Which type of lipid anchored protein is the most elaborate?
- T/F Thioester and Acyl anchors have a broader range of lipids and proteins to bind to
- Name the the lipid anchor specifics for Amide-Linked Myristoyl
- What does it mean for the lipids and proteins of the membrane to exhibit transverse symmetry?
- What does it mean for the lipids and proteins of the membrane to exhibit lateral heterogeneity?
- T/F, Lipid-anchored membrane proteins can be both covalently linked and reversibly bound
- Define Lipid-Anchored Membrane Proteins:
- Name 4 types of lipid-anchored membrane proteins:
- Describe the inside and outside of Wza's structure
- Describe the structure of Wza:
- T/F Alpha helices cannot form transmembrane "barrels"
- Where are porins found?
- Define Porins:
- Name 5 other structural changes that can occur in a transmembrane protein:
- Explain the significance of the "Positive Inside" rule:
- Which type of amino acids are commonly found in the lipid tail interior of the lipid bilayer?
- Which specific protein residues are most commonly found at the interface between the lipid and water?
- Where are charged and polar residues of a protein found in relation to the cell membrane?
- Define Hydropathy Index:
- On a hydropathy plot, which sign indicates hydrophobic (transmembrane) segments?
- What are the two quantities that protein topology is based on?