denaturation proteins Flashcards
What are proteins composed of?
Proteins are polymers of amino acids.
What is the primary structure of a protein?
The sequence of amino acids.
What defines the secondary and tertiary structures of proteins?
The protein’s folded state.
What is the native conformation of a protein?
The state in which the protein is most active and functional.
What forces hold proteins in their native conformations?
- Hydrogen bonds
- Ionic interactions
- Disulfide bridges
- Hydrophobic interactions
What is denaturation?
Changing the conformation of a protein by disrupting its forces, resulting in a loss of protein activity.
What happens to a protein’s solubility during denaturation?
It changes and frequently results in the formation of a solid in the solution.
What are denaturing agents?
Reagents or conditions that can cause denaturation, such as heat, pH changes, alcohol, and heavy metal salts.
How does heat act as a denaturing agent?
It supplies kinetic energy, causing atoms to vibrate and disrupting weak forces like hydrogen bonds.
What is the effect of extremes of pH on proteins?
They can change the charges on amino acid R-groups, disrupting ionic bonds.
How does ethanol function as a denaturing agent?
It forms hydrogen bonds with protein molecules, disrupting their hydrogen bonding.
Why is a 70% alcohol solution preferred for disinfecting?
It penetrates bacterial cell walls effectively, unlike a 95% solution which coagulates proteins at the surface.
What is the effect of heavy metal salts on proteins?
They form strong bonds with disulfide groups, disrupting disulfide bridges and causing precipitation.
Why are substances high in protein used as antidotes for heavy metal poisoning?
They combine with metal ions to form insoluble solids.
What is the purpose of this lab?
To examine four different ways of denaturing protein.
