NURSING ANM AND GNM

Detailed explanation-1: -Both structures are held in shape by hydrogen bonds, which form between the carbonyl O of one amino acid and the amino H of another.

Detailed explanation-2: -The main forces which stabilize the secondary and tertiary structures of proteins are hydrogen bonds, disulphide linkages, van der Waals and electrostatic forces of attraction.

Detailed explanation-3: -The quaternary structure is also stabilized by the non-covalent interactions and disulfide bonds as in the tertiary structure, where more than one polypeptide is held together to form a single functional unit called multimer.

Detailed explanation-4: -The Hydrophobic Effect Is a Principal Force Stabilizing Tertiary and Quaternary Structures. In addition to ionic, hydrogen-bonding, and van der Waals interactions, an important driving force for protein folding is the hydrophobic effect.

Detailed explanation-5: -The tertiary structure of a protein refers to the overall three-dimensional arrangement of its polypeptide chain in space. It is generally stabilized by outside polar hydrophilic hydrogen and ionic bond interactions, and internal hydrophobic interactions between nonpolar amino acid side chains (Fig. 4-7).