Title :
Effect of hydration on molecular stability of bone collagen
Author :
Tamilselvan, A. ; Zhang, D.
Author_Institution :
Dept. of Mech. & Aerosp. Eng., Rutgers Univ., Piscataway, NJ, USA
Abstract :
The mechanical properties of bone degrade as we age and this effect is partially contributed by the decrease of bone water content during aging. In this paper, we study the role water plays in stabilize the molecular structure of collagen. Collagen type I is the major constituent of bone. The stability of collagen triple helix is evaluated with and without hydration utilizing both molecular mechanics and finite element methods
Keywords :
biochemistry; bone; finite element analysis; hydrogen bonds; molecular biophysics; molecular configurations; molecular force constants; proteins; solvation; Collagen type I; MM2 force field; bond deformation; bone collagen; bone water content; collagen triple helix stability; conformational energy searching; energetically preferred conformations; fibrous proteins; finite element method; glycine; heterotrimer; hydration effect; hydrogen bonds; imino acid residues; interstitial water; mineralization; molecular mechanics; molecular scaffold; molecular stability; natural aging process; structural stability; water bridges; water loss kinetics; Amino acids; Biomechanics; Bonding; Bones; Bridges; Hydrogen; Joining processes; Minerals; Peptides; Stability;
Conference_Titel :
Bioengineering Conference, 2002. Proceedings of the IEEE 28th Annual Northeast
Conference_Location :
Philadelphia, PA
Print_ISBN :
0-7803-7419-3
DOI :
10.1109/NEBC.2002.999533
