The secondary and tertiary structures of proteins arise from the inherent properties of polypeptide bonds, which are not straight and allow for rotation, influenced by bond angles and the presence of hydrogen bonds. These structures result from weak forces, including ionic bonds, van der Waals forces, and hydrogen bonds, which dictate the protein's conformation. The lowest energy state, determined by the total energy of the molecule, typically represents the most stable conformation, though this can vary in living systems. The hydrophobic effect plays a crucial role, with hydrophobic side chains often buried in the protein's core while hydrophilic ones are exposed. This arrangement is facilitated by secondary structures like alpha helices and beta sheets, which help satisfy polar groups through hydrogen bonding. Tertiary structures are thermodynamically driven, seeking a conformation that minimizes Gibbs free energy, and are influenced by environmental factors such as temperature. Proteins are dynamic, constantly adjusting their shapes due to side chain movements.