Protein Structure and Bonds

These flashcards cover the types of bonds and interactions that maintain protein structures and the implications of denaturation.

Hydrogen Bonds

Weak bonds that form between the amine group of one amino acid and the carboxyl group of another, holding protein structures like the alpha helix in shape.

Ionic Bonds

Strong bonds that form between groups with opposite charges, often involving R groups of amino acids that contain carboxyl or amino groups.

Van der Waals Forces

Weak forces that act between any two atoms that are close together, significant in stabilizing the three-dimensional structure of proteins.

Disulphide Links

Strong covalent bonds formed between the R groups of cysteine molecules, contributing to the stability of protein structures.

Denaturation

The process where the protein structure changes as bonds are broken, causing the molecule to unfold and potentially lose its solubility.

Globular Proteins

Proteins that fold into a spherical shape, with hydrophobic R groups typically hidden in the interior, making them soluble in water.

Hydrophobic Interactions

Attractions between non-polar R groups of amino acids that help maintain protein structure by excluding water.

Tertiary Structure

The three-dimensional shape of a protein, formed by the folding of the polypeptide chain, stabilized by various types of bonds and interactions.

Quaternary Structure

The arrangement of multiple polypeptide chains in a protein, influencing its overall shape and functionality.

pH Sensitivity

The susceptibility of proteins to changes in shape or denaturation due to variations in pH, affecting ionic bonds within the structure.