Answer:
Choosing protein as macromolecule.
Explanation:
The given environmental changes can lead to structural changes in protein as well:
pH - Several amino acids contain sidechains with practical gatherings that can promptly pick up or lose a proton. Changes in pH would prompt an adjustment in the charge of the amino acids, prompting charge-charge attraction or repilsion between non-interfacing amino parts.
Temperature - High temperatures can prompt protein denaturation. Warmth can upset hydrogen bonding and hydrophobic interactions.
Reduction or oxidation Environment - Some tertiary structure of protein folding is held by disulfide linkages. Reducing agent will lead to unfolding by introducing itself to break disulfide bonds.
Effect of these change: Sequence of amino acid and structure of protein molecule form determines function, any slight change to a protein's structure may result in the protein to become dysfunctional or produce different product.
Answer:
The answer is d. carbon-12, potassium, and argon
the (drug and control) are the variable that you will change throught the conducted investigation.
Answer:
In the lysogenic cycle, the viral genome gets incorporated into the host genome and replicates with the host genome. In the lysogenic cycle, no proteins and enzymes of the virus are formed while in the lytic cycle protein of viral capsid form and new phages generate in the host cell.
So as the viral genome integrates into the host genome in the lysogenic cycle, therefore, it is difficult for any drug to differentially act on the viral genome. So there are great chances for drugs to target the host genome in the host cell.
But in virus that replicates through lytic cycle drugs can selectively act on viral enzyme and proteins. Therefore it is difficult to make a drug that affects lysogenic virus.
