Article
Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine.
Proceedings of the National Academy of Sciences of the United States of America - 11 Apr 2000
Beck K, Chan V C, Shenoy N, Kirkpatrick A, Ramshaw J A, Brodsky B
Abstract excerpt
Mutations resulting in replacement of one obligate Gly residue within the repeating (Gly-Xaa-Yaa)(n) triplet pattern of the collagen type I triple helix are the major cause of osteogenesis imperfecta (OI). Phenotypes of OI involve fragile bones and range from mild to perinatal lethal. In this study, host-guest triple-helical peptides of the form acetyl-(Gly-Pro-Hyp)(3)-Zaa-Pro-Hyp-(Gly-Pro-Hyp)(4)-Gly-Gly-amide...
Topics
- Amino Acid Substitution
- Circular Dichroism
- Collagen
- Glycine
- Humans
- Osteogenesis Imperfecta
- Peptide Fragments
- Phenotype
- Protein Conformation
- Thermodynamics