3. When you think about the primary structure of the mannose-6-P receptor, assuming that it is anintegral membrane protein with one membrane-spanning domain and assuming that it has a ERSS, whatare all of the different protein domains that must be present in this protein's primary structure to get itto where it needs to go and to carry out all of the functions/activities? (Draw a schematic of the proteinstructure/sequence and explain each region).

The internal amino acid sequences in the membrane protein carries the information that determines…

Answered: 3. When you think about the primary…

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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5.. A sample of cells has a total receptor concentration of 25 mM. Ninety percent of the receptors have bound ligand and the concentration of free ligand is 125 µM. Calculate the K for the receptor ligand interaction. (a) What is the AG° for binding for this interaction at 25°C?
What type of signal sequence(s) would be used to create the ACE2 (type 1) integral membrane protein?
6. Define a receptor tyrosine kinase and distinguish it from a serine/threonine kinase. (As we discuss ANY kinase in signalling pathways, pay close attention to what type of kinase it is...does it phosphorylate serene/threonine resides or tyrosine residues?)
Why are proteins unfolded in order to enter the mitohondria during post-translational transport? Which transport proteins do they enter through? Is it a receptor? Does it take energy to bring the unfolded protein in? What kind of proteins are brought into the mitochondria and why? Also, why are the proteins folded back up once it enters the mitochindria? Please help me understand this a little bit better...Thank you
Ion channels are formed by a particular kind of membrane protein that allows the passage of a specific ion (or ions) under certain conditions. This type of protein is most likely a(n) a. peripheral membrane protein with additional hydrophobic domains b. integral membrane protein with a transmembrane domain c. a cholesterol-like molecule that is positioned in the phospholipid bilayer d. membrane phospholipid with hydrophilic head group e. soluble enzyme anchored to a scaffolding protein on the cytoplasmic side of the plasma membrane
Inside of skeletal muscle cells are voltage-controlled calcium ion (Ca2+) gate proteins. These are integral for the contraction mechanisms of skeletal muscle. A picture of them is shown below. These are regulated by voltage, as indicated above. How would voltage serve to open or close these gates? Voltage is a component of hydrogen bonds, which is necessary to maintain the secondary structure of the protein; without voltage, the protein starts to chemically degrade. Voltage actually does not serve as the direct mechanism of opening or closing gated proteins. Changing the voltage changes whether the R groups are charged or not, which alters the actual primary structure of the protein Changing voltage changes the nature of the tertiary structure, causing the protein to change its shape to open or close.
2.2. Draw a schematic pathway, specifically naming components and state (in a few sentences) how membrane bound Phosphatidylinsoitol (PI) leads to the regulation of protein function by the phosphorylation.
9. Shown below is a binding pocket for a protein with a ligand bound. The ligand interacts with a serine and a valine side chain. ligand a. Briefly explain, in terms of Ka, the effect of a mutation that replaces the serine residue with a valine residue. b. Briefly explain, in terms of Kd, the effect of a mutation that alters the ligand (as seen below) binding to the original, unmutated, binding site. :0: ligand 2
Protein A binds to Ligand X with a Kd of 1 μM. Protein B binds to Ligand Y with a Kd of 100 nM. Which of the following statements is TRUE? A. Protein A binds Ligand X ten times tighter than Protein B binds Ligand Y B. At a sufficiently high concentration of ligand, the binding becomes irreversible C. When the concentration of Ligand X is 1 μM, 50% of Protein A is bound to ligand D. Protein B binds to Ligand Y with a Kd of 1 × 10-8 mol/L. E. When both binding reactions are at equilibrium, Protein A has more Ligand X bound than Protein B has ligand Y bound The answer is C, could you show how to get the answer? Thanks
1. List four classes of membrane-associated proteins and briefly describe the differences between them. 2. What are 3 types of modifications that can anchor proteins to the membrane? How do they link to the proteins they anchor?
1. You are working on identifying novel proteins associated with the plasma membrane and you isolate XYZ1. Protein sequencing shows XYZ1 is comprised of: MGASSCSELRSSAFALSERSDKSSAVLLIVLGVMAVGIYLLVTMVLIIGTSANRASGSKD SESMSTLECAAPNDSAA a. Based on the sequence. Do you predict this is a peripheral membrane protein or an integral membrane protein? (Hint: use the Hydropathy plot generator on Expasy using default settings to help answer this question.) b. You decide to conduct an experiment to further assess how the protein is connected to the PM. The experiment is conducted by either 1) treating intact cells with chymotrypsin, 2) by disrupting the plasma membrane such that chymotrypsin has access to both sides of the plasma membrane, or 3) by using detergents to remove all lipid bilayers and treating the proteins such that chymotrypsin will have access to -Chym. Cond. 1 - +Chym. Cond. 2 Cond. 3 the entire length of the protein. The treatments are run on an SDS-PAGE gel (together with an…

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