Drawn below is a schematic of a transmembrane protein.ExtracellularCellmembraneCytosolic 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.

Introduction: A membrane protein is a protein molecule that is connected or linked with the…

Answered: Drawn below is a schematic of a…

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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Similar questions

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?
Many transmembrane proteins have a large series of hydrophobic amino acids such as those in the middle of the protein (around b). Why would this make sense, and where would you expect these to be located in the final protein structure?
Transmembrane portrudes on both sides. Integral protein is in the width of the bilayer and may portrude on one or both sides of the bilayer. Is Transmembrane Protein semi-similar to Integral Proteins? How can we tell the difference of the two?
What differences would you expect in the structure of a membrane bound protein versus a cytosolic protein?
The compositions of the inner and outer surfaces of the lipid bilayer are different. Why do these differences exist and how might they be of use to a living cell?
The tertiary structure of a protein is the 3-dimensional folding of the polypeptide chain. What types of bonds support the folding of proteins into this level of protein structure? Also, how do these bonds/interactions impact how a protein folds and its surface properties? Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.
Proteins may be bound to the exoplasmic or cytosolic face of the plasma membrane by way of covalently attached lip- ids. What are the three types of lipid anchors responsible for tethering proteins to the plasma membrane bilayer? Which type is used by cell surface proteins that face the external medium? By glycosylated proteoglycans?
What typical structure[s] is/are found in integral membrane proteins – how do they span themembrane?
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.
Explain how can one predict the number of transmembrane domains (TM helices) in an integral membrane protein. Note: For the above question, I only seek for an original answer no more than six sentences.
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 7.4

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