Exchange of the Structural Water and Molecular Dynamic in Collagen

Water has been found to be essential in the maintainance of collagen in its native conformation and is considered as an integral element of the collagen structure. The collagen triple helix differs from both the α-helix and the β-sheet structures in that not all hydrogen bonding sites on the backbone are occupied within the macromolecular structure. Only every third C=O and NH group of the backbone is involved in intramolecular hydrogen bonding. Water molecules stabilize the triple helical structure by intramolecular bridges by binding to the unoccupied hydrogen donor and acceptor groups on the protein backbone (Traub 1971; Ramachandran 1976).