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Concept explainers
To determine: The reason that misfolded proteins are a problem for a eukaryotic cell.
Introduction: Protein folding is a process through which a protein chain acquires its 3-dimensional structure. All protein molecules are a heterogeneous unbranched chain of amino acids. These chains undergo coiling and folding to perform their biological function.
To determine: The ways by which eukaryotic cell overcome the accumulation of misfolded proteins.
Introduction: Protein misfolding is a phenomenon in which certain proteins become structurally abnormal. These abnormal proteins disrupt the function of cells, tissue, and organs of the body. These misfolded proteins cause severe disorders.
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Chapter 14 Solutions
Concepts of Genetics Plus Mastering Genetics with Pearson eText -- Access Card Package (12th Edition) (What's New in Genetics)
- Each type of molecule listed below is recognized by a specific class of nuclear import receptor (importin) or nuclear export receptor (exportin). For each type of molecule, state whether you think it is recognized by an importin or exportin and explain why (in terms of where that molecule is synthesized, what that molecule does, and where it does it). (a) RNA polyermase II: (b) ribosomal protein: (iii) †RNA:arrow_forwardWhy might some cells in the body, such as those in bonemarrow, be more susceptible to ribosomal protein mutations than other cell types?arrow_forwardIn 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.arrow_forward
- What are histone acetyl transferases (HATs)?arrow_forwardBased on the N-terminal amino acid sequence, what is the approximate half-life of the protein after methionine is cleaved off?arrow_forwardWild-type E. coli cells can synthesize all 20 common amino acids, but some mutants, called amino acid auxotrophs, are unable to synthesize a specific amino acid and require its addition to the culture medium for optimal growth. Besides their role in protein synthesis, some amino acids are also precursors for other nitrogenous cell products. Consider the three amino acid auxotrophs that are unable to synthesize glycine, glutamine, and aspartate, respectively. Match each nitrogenous product with the mutant or mutants that would fail to synthesize it. Each mutant may fail to synthesize more than one nitrogenous product, and some nitrogenous products may fail to be synthesized by more than one mutant. glycine auxotrophs glutamine auxotrophs aspartate auxotrophs Answer Bank adenine nucleotides cytosine nucleotides guanine nucleotides uridine nucleotidesarrow_forward
- Consider the mechanism of the enzyme RNase: What would happen to the Km (i.e., would it increase, decrease, or stay the same) if the his12 was mutated to a lysine? Explain. What would happen to the Kcat (i.e., would it increase, decrease, or stay the same) if the his12 was mutated to a valine? Explain.arrow_forwardA certain membrane protein is found on the ER membrane with the N-terminus on the ER side of the membrane and the C-terminus on the cytosol side of the membrane. The protein contains three transmembrane domains. What would be the orientation of the protein across the ER membrane if the gene were mutated such that the third transmembrane domain coded for hydrophilic amino acids? (B) (D) N с N N =481 (- rough ER membrane C ER LUMEN CYTOSOL (A) Choose one: Orientation A Orientation B Orientation C O Orientation D (C) N Carrow_forwardWhat factors can promote protein misfolding in cells?arrow_forward
- Describe the function of the Bicoid protein. Explain how its ability to exert its effects in a concentration-dependent manner is a critical feature of its function.arrow_forwardHow does the cell ensure that a specific amino acid (say, valine) attaches itself only to the one tRNA molecule that is specific for valine? (A) Proteins called aminoacyl DNA synthetases are responsible for bringing together the proper pair. The enzymes match the amino acid and one of the correct DNA molecules carrying the right anticodon. (B) Lipids called aminoacyl tRNA synthetases are responsible for bringing together the proper pair. The lipid binds the amino acid and one of the correct tRNA molecules carrying the right codon. (C) Enzymes called aminoacyl tRNA synthetases are responsible for bringing together the proper pair. The enzymes match the amino acid and one of the correct tRNA molecules carrying the right anticodon. (D) Enzymes called peptidyl mRNA synthetases are responsible for bringing together the proper pair. The enzymes match the amino acid and one of the correct mRNA molecules carrying the right anticodon.arrow_forwardThe steroid progesterone has an important role in the female reproductive system. Researchers interested in studying membrane progestin receptors (MPRS) developed a method to produce and purify the protein in active form. First, the researchers devised a way to prepare a specific MPR known as hMPRA using the machinery of yeast cells. In order to facilitate purification and identification in later studies, they manipulated the yeast cells so that they attached two different tags to the C-terminal end of the protein. The first tag, Compound 1, is a peptide sequence that acts as an epitope, part of a much larger peptide sequence that is recognized by the immune system. The second sequence consisted of six consecutive histidine residues (His). This sequence binds tightly to Ni2+ cations. In chromatography, (His), tag labeled proteins can be eluted from Ni²+. supported columns by adding a small molecule to the eluent that mimics the side chain of histidine.…arrow_forward
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