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

fYear

2002

fDate

2002

Firstpage

197

Lastpage

198

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;

fLanguage

English

Publisher

ieee

Conference_Titel

Bioengineering Conference, 2002. Proceedings of the IEEE 28th Annual Northeast

Conference_Location

Philadelphia, PA

Print_ISBN

0-7803-7419-3

Type

conf

DOI

10.1109/NEBC.2002.999533

Filename

999533