Concept explainers
To determine: The cells that best survived at 10-6 grams per liter concentration of RIP.
Introduction: Ribosome-inactivating proteins (RIPs) inactivate the ribosomes and prevent protein synthesis in a cell. It removes adenine base from ribosomal rRNA that forms the part of binding site for proteins involved in GTP. This results in inability of ribosome to bind to these proteins and protein synthesis stops. The toxic RIPs have a domain that makes them enter into another that interferes with ribosome. They have antiviral and anticancer properties, and used to design drugs for HIV and cancer.
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Chapter 9 Solutions
Bundle: Biology: The Unity and Diversity of Life, Loose-leaf Version, 14th + LMS Integrated for MindTap Biology, 2 terms (12 months) Printed Access Card
- Figure 15.16 Many antibiotics inhibit bacterial protein synthesis. For example, tetracycline blocks the A site on the bacterial ribosome, and chloramphenicol blocks peptidyl transfer. What specific effect would you expect each of these antibiotics to have on protein synthesis? Tetracycline would directly affect: tRNA binding to the ribosome ribosome assembly growth of the protein chain Chloramphenicol would directly affect tRNA binding to the ribosome ribosome assembly growth of the protein chainarrow_forwardAnalyse and interpret the SCAM data in Fig. 1, and make a table (remember to include a legend) to indicate where each amino acid is located (cytoplasm, membrane, periplasm).arrow_forwardMCQarrow_forward
- In the: Mutation of the 28S RNA preventing the binding of the 40S with 60S ribosomes Explain: (a) What is the process affected? (b) What is the Effect on the process? (c) Does it affect prokaryotes, eukaryotes or both?arrow_forwardeading list Cells have oligosaccharides displayed on their cell surface that are important for cell-cell recognition. Your friend has discovered a transmembrane glycoprotein, GP1, on a pathogenic fungal cell that is recognized by human immune cells. He decides to purify large amounts of GP1 by expressing it in bacteria. To his purified protein he then adds a branched 14-sugar oligosaccharide to the asparagine of the only Asn-X- Ser sequence found on GP1. Unfortunately, immune cells do not seem to recognize this synthesized glycoprotein. What's a likely explanation for this problem? O The oligosaccharide needs to be further modified before it's mature. O The oligosaccharide should've been added one sugar at a time. O The oligosaccharide needs a disulfide bond. O The oligosaccharideehould've been added to the serine instead of the asparagine.arrow_forwardOnce the chains of peptides that make up lysyl-tRNA synthetase protein are synthesized in ribosomes, lysyl-tRNA synthetase needs to have the proper active site in order to perform its function, explain the process of protein folding necessary to have a proper 3-D structure, include effect of thermodynamics and different states in folding, including what happen when there are prolines that form peptide bonds with other amino acids, and any disulfide bridgesarrow_forward
- In the: Inhibition of splicing by ribozymes Explain: (a) What is the process affected? (b) What is the Effect on the process? (c) Does it affect prokaryotes, eukaryotes or both?arrow_forwardFull length resilin that is not in a cell is thought by some to form a tertiary structure of this form (picture attached) The yellow portions represent exon 1 and the blue portions exon 3. These structures assemble into a kind of lattice or network. In full length resilin, stress in the form of mechanical pressure or heating to remove water results in a tighter network that excludes any water internally. How might this behavior of resilin produce its ‘elasticity’? Explain how the looser water containing structure and the tighter water excluding structure may give us a mechanism for the elasticity.arrow_forwardThis answer is incorrect pls provide the right answer and explanationarrow_forward
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