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When using combination antibiotic therapy, it is important to administer drugs that work synergistically as possible. Which of the following represents a combination with known synergism?
- A beta-lactam and an aminoglycoside
- A penicillin and a cephalosporin
- Two drugs in which the second drug will displace the first from plasma protein-binding sites.
- Two drugs that are eliminated by different routes
- Two drugs that work on the same step in a
metabolic pathway.
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- In the discovery of new drugs, the chemical and physical properties of a molecule are very important to be determined. All of the following are physical and chemical properties that are important in drug discovery EXCEPT….A. route of administrationB. fat/water partitionC. molecular steric hindranceD. pHE. pKa Secretion of acid ions from gastric acid, is one of the drug distribution processes by...A. Passive diffusion with facilitiesB. passive diffusionC. dissolves in lipids that make up the membraneD. pinocytosisE. active diffusionDefine the following terms:a. proenzymeb. positive cooperativityc. negative cooperativityd. zymogene. free radicalDefine the following terms: a. genetic control b. proenzyme c. zymogen d. positive cooperativity e. negative cooperativity
- Which of the following statements about antibiotics is TRUE? a) Antibiotics are used to disinfect bench tops.b) An antibiotic is a type of antiseptic.c) Some antibiotics inhibit the growth of a pathogen and do not kill it.d) Some antibiotics work by binding the 40S ribosomal subunit.e) Antibiotics are used to treat fungal infections.The human intestinal tract is home to a vast, diverse microbial community. The bacteria that comprise this microbial community serve a number of important, beneficial functions. However, some bacterial species have been suggested to play a role in certain forms of cancer. One such bacteria is Fusobacterium nucleatum (i.e., F. nucleatum). Investigators wishing to study the role of F. nucleatum in colorectal cancer developed a new assay for detecting these bacteria in tumor tissue. In controlled experiments, the test was highly sensitive in detecting F. nucleatum and also had high specificity. To examine consistency in their test findings, the investigators also conducted repeat tests in 50 tissue samples. From these repeat tests, the investigators observed that the overall number of samples in which F. nucleatum was detected was almost identical (10 out of 50 on the first test vs. 11 out of 50 on the repeat test); for 9 samples, F. nucleatum was detected on both the initial and the…Choose an enzyme or therapeutic protein of high market value. Explain the biological process used to produce it in terms of the cell line used, mode (batch, semi-batch, etc), and purification steps used.
- The site on an enzyme that will bind the substrate is called the active site. activation site. prosthetic group. catalyst. metastable site.The anitbiotic penicillin is effective against bacteria by _____. inhibiting the sunthesis of peptidoglycan blockimng the adhesion of the capsule to the substrate inhibiting the formation of fimbriae blocking the operation of the proton pump Interfering with conjugationdescribe the molecular switches involved in microbial acute/prolonged starvation response. give one research article link
- 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?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 are antibiotics ineffective in treating the common cold and other virus infections?Match the listed possible protein functions to the example of that function from the list. Structural support Enzymes Defense Communication Transport I. The movement of cations across the cell membrane is carefully controlled through gated channels to ensure osmotic balance. II. Lysozyme is found in tears and saliva where it acts as an antimicrobial enzyme. III. RNA polymerase converts individual nucleotides into mRNA from the DNA template in the nucleus. IV. Growth hormone is a peptide secreted from the brain that can bind to receptors in the body to stimulate cellular growth. V. Keratin is an aggregate protein found in the hooves of rumnant animals as hard protective coveres at the ends of limbs. VI. None of