. The structure of certain porin proteins isorganized into an interesting beta-barrel, in which each beta strand spans the lipidbilayer at an ~45° angle. Using this information, together with general dimensions of thelipid bilayer, what would be the approximate number of amino acids found within a betastrand in an aquaporin protein complex? Explain how you arrive at your answer.

IntroductionStructureAquaporin have structure consisting of 6 member helical structure forming…

Answered: . The structure of certain porin…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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(c) The tube and cylinder diagram to the right illus- trates schematically the potassium channel protein from a bacterium. This channel protein consists of four identical polypeptide chains each comprised of 119 residues. The cyan ribbon illustrates only two of the polypeptide chains. The relative positions of 4 α-helices, one from each poly- peptide chain, are shown as cylinders. The red sphere in the central part of the diagram shows the position of a potas- sium ion identified by X-ray structure analysis. A cesium ion (green sphere) was also found to be stabilized in the same position when cesium chloride was introduced into the crys- tals. The cylinders each represent an α-helix running from Tyr62 to Thr74. Considering the position of the potassium ion, in- dicate on one of the cylinders at which end of the cylinder residue Tyr62 is found and at which end residue Thr74 is found. Explain the basis of your answer? Ala23 Thr119 (d) The N- and C-terminal residues of one of the…
Roughly sketch the hydropathy plot for the given hypothetical membrane protein. Follow the color assignment of the helical domains and properly label your plot and axes (NB: Only a rough sketch is being asked. No need be exact with the hydropathy indices and residue numbers). CO-
Hydropathy plot analysis of your protein of interest reveals a single, prominent hydrophobic peak. However, you later discover that this protein is soluble and not membrane associated. Explain how the hydropathy plot may have been misleading.
I'm honestly confused on where to start with this question. I think it has something to do with the residues per turn but can you please explain and show detailed work on the the problem. Researchers have discovered a new membrane protein that has three transmembrane domain αhelixes that span the lipid bilayer. a. If the lipid bilayer is 30 Å thick, what is the smallest number of amino acid residues that can be in each α-helixes for them to be long enough to span the bilayer? b. If one of the three α-helixes is titled at a 32° angle relative to an axis perpendicular to the surface of the lipid bilayer, what is the smaller number of amino acid helixes required for that helix to still span the lipid bilayer? c. How many hydrogen bonding interactions would there be in the smallest possible tilted transmembrane α-helix? d. If the tilted α-helix was a 310 helix instead how many amino acid residues would be required to span the lipid bilayer? How many amino acid residues would be required if…
Draw a hydropathy plot and a 2D protein cartoon for a protein that passes through the lipid bilayer 6 times..
Researchers have discovered a new membrane protein that has three transmembrane domain αhelixes that span the lipid bilayer.a. If the lipid bilayer is 30 Å thick, what is the smallest number of amino acid residues thatcan be in each α-helixes for them to be long enough to span the bilayer?
The plasma membrane of E. coli is about 75% protein and 25% phospholipid by weight. How many molecules of membrane lipid are present for each molecule of membrane protein? Assume an average protein Mr of 50,000and an average phospholipid Mr of 750. What more would you need to know to estimate the fraction of the membrane surface that is covered by lipids?
Drawn below is a schematic of a transmembrane protein. Extracellular Cell membrane Cytosolic side (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
Drawn 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.
Membrane lipid molecules exchange places with their lipid neighbors every 10–7 second. A lipid molecule diffuses from one end of a 2-μm-long bacterial cell to the other in about 1 second. Are these two numbers in agreement (assume that the diameter of a lipid head group is about 0.5 nm)? If not, can you think of a reason for the difference?
Nearly all bacteria contain peptidoglycan. Review the structure of peptidoglycan by selecting the correct characteristics listed below. Check All That Apply Polymer of alternating N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM) Contains a tetrapeptide that extends from N-acetylglucosamine (NAG) Contains D-amino acids not found in proteins All bacteria use a peptide interbridge to connect the sugar strands Peptidoglycan is a strong and rigid structure
Your research advisor would like you to measure the movement of a protein X using FRAP. The results of your FRAP experiment are shown below. What can you conclude? Fluorescence Intensity (Arbitrary Units) Time (Seconds) Time point of exposure to an intense laser Protein X appears to be completely immobilized in the membrane Protein X appears to be partially immobilized in the membrane You cannot make predictions about the mobility of Protein X with these data Protein X appears to be completely mobile in the membrane

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