B1.2 HL Proteins Flashcard

Front

What type of bonding is involved in the secondary structure of proteins?

Back

Hydrogen bonding is responsible for the secondary structure of proteins, forming alpha helices and beta sheets.

Front

What effect do polar and non-polar amino acids have on the tertiary structure of proteins?

Back

Polar and non-polar amino acids affect how proteins embed within a membrane, influencing their overall structure and function.

Front

What makes an amino acid hydrophilic?

Back

An amino acid is hydrophilic if it has a polar or charged R-group, allowing it to interact with water.

Front

Which type of bond is responsible for the folding of a protein into its tertiary structure by forming a hydrophobic core?

Back

Hydrophobic interactions are responsible for the folding of proteins into their tertiary structure, creating a hydrophobic core.

Front

What is an example of a conjugated protein?

Back

Hemoglobin is an example of a conjugated protein, as it contains a heme group in addition to its polypeptide chains.

Front

Define primary structure of proteins.

Back

The primary structure of a protein is the linear sequence of amino acids in a polypeptide chain.

Front

What role do disulfide bridges play in protein structure?

Back

Disulfide bridges stabilize the tertiary structure of proteins by forming covalent bonds between cysteine residues.

Front

Explain the significance of the R-group in amino acids.

Back

The R-group, or side chain, determines the properties of an amino acid, influencing protein structure and function.

Front

What is the difference between polar and non-polar amino acids?

Back

Polar amino acids have R-groups that can form hydrogen bonds with water, while non-polar amino acids have R-groups that are hydrophobic.

Front

How do temperature and pH affect protein structure?

Back

Temperature and pH can denature proteins, disrupting their secondary, tertiary, and quaternary structures.