Collagen stability, hydration and native state.
Molecular dynamics simulations of a collagen-like peptide (Pro-Hyp-Gly)4-Pro-Hyp-Ala-(Pro-Hyp-Gly)5 have been done in order to study the contribution of the hydration structure on keeping the native structure of collagen. The simulation shows that the absence of water produces a distortion on the molecular conformation and an increase in the number of intra-molecular hydrogen bonds. This is in agreement with previous experimental results showing the stiffness of collagen under severe drying and its increase in the thermal stability. This dehydrated material does not keep, however, the native structure.
Mogilner
Inés G
IG
Departamento de Ciencias Biológicas, Instituto de Física de Líquidos y Sistemas Biológicos (IFLYSIB) CONICET-UNLP-CIC, 59 No. 789 C.C. 565, Facultad de Ciencias Exactas UNLP Universidad Nacional de La Plata, 1900 La Plata, Argentina.
Ruderman
Graciela
G
Grigera
J Raúl
JR
D000596:Amino Acids / Q000737:chemistry; D003094:Collagen / Q000737:chemistry*; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004355:Drug Stability; D006860:Hydrogen Bonding; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D020449:Repetitive Sequences, Amino Acid; D014867:Water
D000596:Amino Acids; D010455:Peptides; D014867:Water; D003094:Collagen