How does aqueous Silver nitrate, AGNO3, works against neonatal conjunctivitis (inflammation of the outer eye) due to neonatal bacterial infection? * It hydrolyzes protein in bacteria to amino acids and inactivate it. O It denatures the protein bacteria and kills them. It mutates the genetic make-up of bacteria and transforms them to useful proteins. It oxidizes side chains of cysteine residues to cystine.

How does aqueous Silver nitrate, AGNO3, works against neonatal conjunctivitis (inflammation of the outer eye) due to neonatal bacterial infection? * It hydrolyzes protein in bacteria to amino acids and inactivate it. O It denatures the protein bacteria and kills them. It mutates the genetic make-up of bacteria and transforms them to useful proteins. It oxidizes side chains of cysteine residues to cystine.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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Similar questions

Draw the structure of the short protein: glutamate-leucine-serine.
H₂N CH3 ZI O OH Which of the following statements is True? SH ZI O OH NH₂ All amino acid residues are chiral. The C-terminus contains a basic residue. It cannot form disulfide linkage. The N-terminus is Ser. Assuming this is a DNA-encoded polypeptide, then all chiral centres are S.
Draw the Lewis structure of the peptide "YQRWGLA"
The primary structure of a protein is given by what? O a. The number of different functional groups involved O b. The specific folding of the polypeptide chain O c. Hydrogen bonding between backbone segments O d. The sequence of amino acids in the polypeptide chain
What process results in cleavage of peptide linkages in a protein? O esterification O hydrolysis O denaturating O hydrogen bonding
Explain about cysteine residues. How many cysteine residues a α-Keratins has ?
Explain about Amino Acids and Proteins?
What do your findings suggest about the stability of proteins in the presence of organic solvents?
`The chemical properties can differ between amino acids due to what main factor? carboxylic acid group R group (side chain) molecular weight armine group
On the basis of polarity, what are the four types of side chains found in the standard amino acids? Draw one of the standard amino acids as an example and indicate the types of side chains
8. From Figure 3, identify the noncovalent force that dominates between the two interacting functional groups indicated by the blue letters d. а. b. е. С.
What are the essential amino acids and how does the body get them? Give an example of one of them and how it can be obtained. Briefly discuss why they are important to overall health and the consequences (health disorder) if they are missing from the diet. Why is a protein's structure important? What can happen if there are any changes?