What can you infer about the structure and cellular localization of the protein below based on its hydropathy index? 100 120 140 160 Resdue nunter O A, It is a cytosolic protein O B. It is a lysosomal enzyme that works in the lumen of the lysosome. OC.It is a cytosolic protein with a single-pass transmembrane domain | surface but may also be found In the ER, Golgi, or O D. It is a multi-pass transmembrane protein that will be ultimately found on the lysosomal membranes.

What can you infer about the structure and cellular localization of the protein below based on its hydropathy index? 100 120 140 160 Resdue nunter O A, It is a cytosolic protein O B. It is a lysosomal enzyme that works in the lumen of the lysosome. OC.It is a cytosolic protein with a single-pass transmembrane domain | surface but may also be found In the ER, Golgi, or O D. It is a multi-pass transmembrane protein that will be ultimately found on the lysosomal membranes.

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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Anfinsen studied protein folding using RNaseA. In one experiment we didn’t discuss in class, he heated RNase in the presence of BME, then he transferred the protein out of water into benzene, and cooled the protein in the presence of O2. Under these conditions, did Anfinsen find the protein was active? Justify your answer.
. The structure of certain porin proteins is organized into an interesting beta-barrel, in which each beta strand spans the lipid bilayer at an ~45° angle. Using this information, together with general dimensions of the lipid bilayer, what would be the approximate number of amino acids found within a beta strand in an aquaporin protein complex? Explain how you arrive at your answer.
7. Specificity of membrane transporters. A protein that transports amino acids across the cell membrane was found to bind only a few amino acids efficiently. To find the specificity, many different amino acids and substrate analogs were used as competitive inhibitors in transport studies at pH 5.9 with L-histidine (Km = 10 μM). The Ki values calculated from Lineweaver-Burk plots are shown in the table below. Comparing the structures of L-histidine and the competitive inhibitors (for which most of them, you should know their structures!), what can you conclude about the characteristics of molecules that this transport protein binds at its active site? K; (10-€ M) Amino acid or analog L-Lys L-Arg Gly L-Asp D-His Histamine Dehydrourocanate D-Arg 2 3 285 450 340 390 285 355 HN- + HN + Structure -ΝΗ -NH3 histamine ΝΗ -COO™ dehydrourocanate
1. The CFTR protein is a chloride channel in the cell membrane. Use your understanding of the biochemical properties/categories of amino acids and how they interact with membrane phospholipids to predict the distribution of charged/polar, and non-polar amino acids within the domains of CFTR listed below. Consider one category to include the charged amino acids and the polar amino acids and the other category to include the non-polar amino acids. For each domain, predict which category of amino acids is likely to be most abundant. Also, explain the rationale behind your prediction. Protein domain Prediction (Charged/Polar or Non-Polar amino acids?) Explanation for prediction TMD1 and TMD2 (transmembrane domains, parts 1-12) ECLs and ICLs (extracellular and intracellular loops) NBD1 and NBD2 R
The role of GTP hydrolysis in actin polymerization is similar to the role of ATP hydrolysis in tubulin polymerization: both serve to weaken the bonds in the polymer and thereby promote depolymerization. Is that true or false? why?