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.
Myosin and actin protein filaments attach to each other . Calcium ions release into myofibrilles . Myosin filaments pull on the actin filaments
Approximately twenty-five elements occur naturally on earth. Remaining elements either have to be synthesized or obtained through chemical reactions.
