ONE ultimate destination of a protein produced on an attached ribosome, and ONE general function of the protein (You do not need to identify the specific protein.) • ONE ultimate destination of a protein produced on a free ribosome, and ONE general function of the protein (You do not need to identify the specific protein.)

ONE ultimate destination of a protein produced on an attached ribosome, and ONE general function of the protein (You do not need to identify the specific protein.) • ONE ultimate destination of a protein produced on a free ribosome, and ONE general function of the protein (You do not need to identify the specific protein.)

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter10: From Proteins To Phenotypes

Section: Chapter Questions

Problem 20QP: If an extra nucleotide is inserted in the first exon of the beta globin gene, what effect will it...

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In eukaryotic cells secreted proteins are targeted first to the endoplasmic reticulum and then pass through the Golgi, before being released from secretory vesicles into the extracellular space. A much simpler route would be for ribosomes synthesising secretory proteins to be targeted to a translocon in the plasma membrane, with the protein being secreted directly as it is translated. List three potential advantages of the former, more circuitous, route for protein secretion over the simpler, more direct, alternative route suggested.
In eukaryotic cells, secreted proteins are initially directed to the endoplasmic reticulum and then via the Golgi, where they are released into the extracellular environment through secretory vesicles. A more easier way would be for secretory protein-producing ribosomes to be localised to a translocon in the plasma membrane, with the protein being secreted directly during translation. Consider three possible benefits of the more roundabout method for protein secretion versus the simpler, more straightforward approach indicated.
The BSA precursor protein is 607 amino acids long and has a molecular weight 69.324 kDa. If a eukaryotic ribosome can synthesize an amino acid chain at 2 amino acids/sec, how many seconds would it take for 107 ribosomes to produce 1 pg of BSA precursor?
Assume that during the process of creating the SHH protein an error was made. Instead of producing a 462-amino-acid-long protein, you only make a 20-amino-acid-long protein. Assume the error is detected in the Golgi apparatus. Will this protein be exported into the extracellular space? If your answer is no, what will happen to this protein?
Consider a transmembrane protein that forms a hydrophilic pore across the plasma membrane of a eukaryotic cell, allowing Na+ to enter the cell when it is activated upon binding a specific ligand on its extracellular side. It is made of five similar transmembrane subunits, each containing a membrane-spanning α helix with hydrophilic amino acid side chains on one surface of the helix and hydrophobic amino acid side chains on the opposite surface. Considering the function of the protein as a channel for Na+ ions to enter the cell, propose a possible arrangement of the five membrane-spanning α helices in the membrane.
Using the the enzyme acid hydrolase in the lysosome: What is the final destination in which the protein will function? Which features will the protein receive during its manufacture? What is the primary structure (general)? Where is the primary structure made? Where are the secondary and tertiary structures made? Will the protein travel through any organelles during its manufacture? Which ones? What would be the overall result if some part of the manufacture process went wrong, such that the protein ended up as nonfunctional?
As a researcher who studies cytoskeletal dynamics, you create a microtubule subunit that cannot hydrolyze GTP. How would the critical concentration for the minus end of a polymer formed by these mutant subunits compare to that of the minus end of a fiber formed by normal microtubule subunits? Why? How would the critical concentration for the minus end of a fiber formed by these mutant subunits compare to that of the plus end of a fiber formed by normal microtubule subunits? Why?
The integral membrane protein XYZR has a single alpha helix spanning the membrane. Where was this protein made and what can you say about amino acids that occur/do not occur in the alpha helix versus the domains sticking out on both sides of the membrane?
What is the major differences between bacteria that use anaerobic vs aerobic respiration and the difference between the 2 processes? Common feautures in the genomic sequences that control transcription between prokaryotes and eukaryotes? Describe some processes of active transport across membranes e g facilitated exocytosis endocytosis active transport?
What are the four components for the translocation of protein across endoplasmic reticulum? and briefly explain ORF?
True or false: In the ribosome, a protein enzyme is responsible for connecting the two amino acids attached to tRNAs in the A and P sites?
Which of the following statements best describes a signal peptide? A.A signal peptide is a short amino acid sequence present at the N-terminus of the majority of newly translated proteins destined for the endomembrane system. B.A signal peptide is a long amino acid sequence that is present at the C-terminus of a protein destined for the localization in lumen of the mitochondrial. C.A signal peptide is a glycan that is post-translational added to a protein to target that protein to the proteosome for degradation. D.A signal peptide is a postranslational modification that adds a lipid to a protein to help anchor the protein to a cellular membrane.