5. Which of the following is NOT true about polypeptides? The peptide bond that links the amino acids together is a type of covalent bond formed through dehydration synthesis. If the overall isoelectric charge of a polypeptide is negative, it will be pulled towards the cathode end during gel electrophoresi O The polypeptide chain modified with ubiquitin molecules are tagged for proteasomal degradation In prokaryotic translation, the initial polypeptide chain produced has a formylmethionine amino acid at the N-terminal.

5. Which of the following is NOT true about polypeptides? The peptide bond that links the amino acids together is a type of covalent bond formed through dehydration synthesis. If the overall isoelectric charge of a polypeptide is negative, it will be pulled towards the cathode end during gel electrophoresi O The polypeptide chain modified with ubiquitin molecules are tagged for proteasomal degradation In prokaryotic translation, the initial polypeptide chain produced has a formylmethionine amino acid at the N-terminal.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 7TYK: Which of the following statements about proteins is correct? a. Proteins are transported to the...

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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 chain
Which of the following sequences correctly lists in order the steps involved in the incorporation of a proteinaceous molecule within a cell? protein synthesis of the protein on the ribosome; modification in the Golgi apparatus; packaging in the endoplasmic reticulum; tagging in the vesicle synthesis of the protein on the lysosome; tagging in the Golgi; packaging in the vesicle; distribution in the endoplasmic reticulum synthesis of the protein on the ribosome; modification in the endoplasmic reticulum; tagging in the Golgi; distribution via the vesicle synthesis of the protein on the lysosome; packaging in the vesicle; distribution via the Golgi; tagging in the endoplasmic reticulum
Antibiotics and Protein Synthesis Antibiotics are molecules produced by microorganisms as defense mechanisms. The most effective antibiotics work by interfering with essential biochemical or reproductive processes. Many antibiotics block or disrupt one or more stages in protein synthesis. Some of these are mentioned here. Tetracyclines are a family of chemically related compounds used to treat several types of bacterial infections. Tetracyclines interfere with the initiation of translation. The tetracycline molecule attaches to the small ribosomal subunit and prevents binding of the tRNA anticodon during initiation. Both eukaryotic and prokaryotic ribosomes are sensitive to the action of tetracycline, but this antibiotic cannot pass through the plasma membrane of eukaryotic cells. Because tetracycline can enter bacterial cells to inhibit protein synthesis, it will stop bacterial growth, helping the immune system fight the infection. Streptomycin is used in hospitals to treat serious bacterial infections. It binds to the small ribosomal subunit but does not prevent initiation or elongation; however, it does affect the efficiency of protein synthesis. Binding of streptomycin changes the way mRNA codons interact with the tRNA. As a result, incorrect amino acids are incorporated into the growing polypeptide chain, producing nonfunctional proteins. In addition, streptomycin causes the ribosome to randomly fall off the mRNA, preventing the synthesis of complete proteins. Puromycin is not used clinically but has played an important role in studying the mechanism of protein synthesis in the research laboratory. The puromycin molecule is the same size and shape as a tRNA/amino acid complex. When puromycin enters the ribosome, it can be incorporated into a growing polypeptide chain, stopping further synthesis because no peptide bond can be formed between puromycin and an amino acid, causing the shortened polypeptide to fall off the ribosome. Chloramphenicol was one of the first broadspectrum antibiotics introduced. Eukaryotic cells are resistant to its actions, and it was widely used to treat bacterial infections. However, its use is limited to external applications and serious infections. Chloramphenicol destroys cells in the bone marrow, the source of all blood cells. In bacteria, this antibiotic binds to the large ribosomal subunit and inhibits the formation of peptide bonds. Another antibiotic, erythromycin, also binds to the large ribosomal subunit and inhibits the movement of ribosomes along the mRNA. Almost every step of protein synthesis can be inhibited by one antibiotic or another. Work on designing new synthetic antibiotics to fight infections is based on our knowledge of how the nucleotide sequence of mRNA is converted into the amino acid sequence of a protein. Questions Why is targeting protein synthesis an effective strategy for preventing infection?
Which of the following is not correct regarding protein domains or modules such as the immunoglobulin domain, growth factor domain, and fibronectin domain? each type of domain is found in a variety of proteins O they always have the same function in differend proteins O domains are hypically 40 to 100 amine acids in length O they can be present in multiple copies in the same protein domains of a certain type usuaily have the same tertiary structure
S1.What functional group (pictured below) is used in the formation of ATP, the backbone of DNA, and the plasma membrane? R. - HO- asluolom OgH 910m ansa obyd to inuoms adisi69 101 P- Hnedenoi HO 9tom anisinos H 19w 1639 eniv blut viend ou nontel:oceansied bol-ngtsl s19 1591 a. Amino b. Carbonyl c. Ester d. Phosphate e. Alcohol Sabios onime Tertio of bensemoo Insietib ti aolem tsrll blas onims ns to neg at to quang ly snodibod for ogh quotg
Which of the following is not a helix destabilizer? O Adjacent amino acid residues with big, hydrophobic side chains Presence of Pro and Gly O 10 consecutive acidic amino acid residues O Presence of Ala and Leu
28) peptidyl transferase enzyme activity forms A- peptide bonds between nucleotides B-peptide bonds between amino acids C- phoshodiester bonds between nucleotides D- hydrogen bonds between nucleic acid bases E- phosphodiester Bonds between amino acids
Base excision repair starts with cleavage of the between the damaged base and the deoxyribose. O hydrogen bond ionic interaction O glycosidic bond O phosphodiester bond
6. What is a glycosyltransferase? Choose all that apply Group of answer choices Catalyzes the formation of a bond between a sugar and an amino acid An enzyme that cleaves a glycosidic bond An enzyme that catalyzes the formation of a glycosidic bond An enzyme that transfers nucleotide-sugars from the cytoplasm 7. Which statement(s) is/are true about inverting and retaining glycosyltransferases? a. Inverting glycosyltransferase catalyzes the epimerization of a sugar b. Inverting glycosyltransferase alters the anomeric configuration of the glycosyl donor c. Retaining glycosyltransferase never preserves the anomeric configuration of the glycosyl donor d. Inverting glycosyltransferase switch the order of acceptor and donor. e. An SN1 reaction mechanism results in exclusive retention of stereochemistry of the anomeric carbon
Oe. Lactose, maltose 17 Water can be converted from the liquid status to gas/vapor by high temperature (100°C), which of the following are responsible for increasing the boiling point of water molecule? ut of Select one: O a. Covalent bond and adhesion nestion O b. Hydrogen bond and cohesion O c. Hydrogen bond and salt formation O d. lonization and cohesion O e. Covalent bond and adhesion Protein conformation depends on the... Select one: of O a. R groups of the composing amino acids O b. Carboxyl group COOH ion O c. Number of peptide bonds O d. Phosphate group O e. Amino group NH2
Match the post-translational protein modification to its function. Creates new binding sites by neutralizing positive charges Form protein complexes through quatenary structures Protein localization in the endomembrane system Targets proteins for degradation Creates new binding sites by adding negative charges Lipid anchors Glycosylation Alkylation Polymerization Phosphorylation Aceylation Ubiquitination…
Which statement about N-linked glycosylation is correct? N-linked oligosaccharides are attached to proteins one sugar at the time in the endoplasmicreticulum. N-linked sugars are attached to proteins as a 14 residue oligosaccharide during translation in the endoplasmic reticulum. N-linked sugars are attached to proteins as a 14 residue oligosaccharide during translation inthe cytoplasm. N-linked sugars are attached to proteins as a 14 residue oligosaccharide after translation inthe Golgi apparatus.