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what might cause a protein to become nonfunctional? (click all that apply) a change in the amino acid sequence; the presence of an enzyme that catalyzes the protein’s formation; a decrease in salt concentration near the protein; an increase in salt concentration near the protein; an increase in the ph of the surrounding solution; a change in temperature near the protein; a decrease in the ph of the surrounding solution; the surrounding solution shifts from water to oil
- A change in the amino acid sequence: Alters the protein's primary structure, affecting its folding and function.
- pH changes (increase/decrease): Disrupts ionic bonds and hydrogen bonds in the protein's secondary/tertiary structure, causing denaturation.
- Temperature change: Excessive heat breaks weak bonds (e.g., hydrogen bonds), disrupting the protein's 3D structure.
- Increased salt concentration: Can cause "salting out" or disrupt ion - mediated bonds, leading to denaturation.
- Solvent shift (water to oil): Proteins are adapted to aqueous environments; a non - polar solvent (oil) disrupts their hydrophilic - hydrophobic interactions, causing denaturation.
The presence of an enzyme typically facilitates protein - related reactions (e.g., synthesis/degradation) but does not inherently cause a protein to become nonfunctional (unless the enzyme is a protease, but this is not implied here). A decrease in salt concentration generally does not cause denaturation (unlike an increase).
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- A change in the amino acid sequence
- An increase in the pH of the surrounding solution
- A change in temperature near the protein
- A decrease in the pH of the surrounding solution
- An increase in salt concentration near the protein
- The surrounding solution shifts from water to oil