(a) From the list below, select the amino acid(s) that might by more common in the extracellular domain of this membrane protein and whose side- chain can form hydrogen bonds with the surrounding water molecules. Explain why you selected this option(s). Lysine Serine Phenylalanine Methionine (b) From the list below, select the amino acid(s) that would likely be found in the transmembrane/ membrane spanning domain of this protein and whose side- chain interacts with the lipid bilayer. Lysine Serine Phenylalanine Methionine
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- Identify the following membrane associated proteins based on their structure: (a) tetramers of identical subunits, each with six membrane spanning α helices; (b) trimers of identical subunits, each with 16 β sheets forming a barrel like structure.The K+ channel is an example of a transmembrane protein (a protein that spans the phospholipid bilayer of the plasma membrane). What types of amino acids are likely to be found (a) lining the channel through which K+ passes, (b) in contact with the hydrophobic core of the phospholipid bilayer con- taining fatty acyl groups, (c) in the cytosolic domain of the protein, and (d) in the extracellular domain of the protein?Peripheral membrane proteins are not amphipathic and do not associate with the nonpolar regions of the lipids? Explain why?
- Although proteins rarely if ever flipflop across a membrane, the distribution of membrane lipids between the membrane leaflets is not absolute except for glycolipids. Why are glycosylated lipids less likely to flip-flop?Membranes that contain a significant proportion of cis unsaturated fatty acids are more fluid than similar membraneswith higher levels of saturated fatty acids. Explain.Disulfide bond formation is a regularly observed protien modification that occurs in the lumen of the ER. Explain why disulfifde bond formation is a modification only found in secretory proteins and the extracellular domain of plasma membrane proteins. Furthermore, highlight the advantages disulfide bonds provide to these proteins.
- The hydropathy plot of a particular hyaluronan synthase is plotted by Heldermon et al and is shown below. From this plot, Heldermon et al circled six putative (or predicated) membrane domains (PMDs). Circle the six regions in the plot above you believe could be transmembrane domains of the protein and indicate why you chose those regions. Please include a description of what information a hydropathy plot gives researchers.Of the following cell membrane lipids, which one prefers to reside in the inner leaflet (or inner half) of the membrane bilayer, AND has an overall neutral charge at physiological pH (7.4)? a) PE (phosphatidylethanolamine) is inner-leaflet with an overall neutral charge at pH 7.4 b) SM (sphinogomyelin) is inner-leaflet with an overall neutral charge at pH 7.4 c) PS (phosephatidylserine) is inner-leaflet with an overall neutral charge at pH 7.4 d) PC (phosphatidylcholine) is inner-leaflet with an overall neutral charge at pH 7.4Many transmembrane proteins are oligomeric, with several identical subunits. The oligonmers are usually found to have some form of C, symmetry, rather than D, or any higher order. Suggest a reason for this observation.
- ILLUSTRATIONS For each of the given proteins: Draw the final location of the following proteins after being translocated. Label the organelle (as well as the organelle parts/compartments) and the cytosol (if necessary) in order to clearly depict the protein's location and orientation. Label the amino and carboxyl ends of the protein. Below your drawing, indicate: . . a. the receptor/s b. the energy source c. if there is signal peptide cleavage or none E. Mitochondrion H₂N-MTS ITS* "Internal targeting sequence that has no cleavage site -COOH SALEDrawn below is a schematic of a transmembrane protein. Extracellular Cell membrane Cytosolic side (a) When this transmembrane protein is embedded in the lipid bilayer, what is the highest order of structure (choose from primary, secondary, tertiary and quaternary) of this protein? Explain why you selected this option.Many transmembrane proteins are oligomeric, with several identical subunits. The oligomers are usually found to have some form of Cn symmetry, rather than Dn or any higher order. Suggest a reason for this observation.