Question

List the 4 "weak" forces that contribute to tertiary structure.

A) Hydrogen bonding, hydrophobic interactions, ionic interactions, van der Waals forces
B) Covalent bonding, disulfide bridges, peptide bonds, hydrogen bonding
C) Ionic interactions, hydrophobic bonds, van der Waals forces, peptide bonds
D) Hydrogen bonding, covalent bonding, disulfide bridges, van der Waals forces

Answer 1

The tertiary structure of a protein is stabilized by hydrogen bonding, hydrophobic interactions, ionic interactions, and van der Waals forces, which are all non-covalent interactions necessary for protein folding.

Step-by-step explanation:

The four 'weak' forces that contribute to the tertiary structure of a protein are hydrogen bonding, hydrophobic interactions, ionic interactions, and van der Waals forces. These non-covalent interactions are essential for the three-dimensional folding of a protein molecule which determines its function. Hydrogen bonding occurs between partially positive hydrogen atoms and electronegative atoms. Hydrophobic interactions are between nonpolar molecules that group together to avoid water. Ionic interactions are between positively and negatively charged side chains of amino acids. Van der Waals forces are weak attractions caused by temporary fluctuations in electron density.