Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks.
Open Access
- 1 August 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (23) , 13995-14000
- https://doi.org/10.1016/s0021-9258(18)77447-4
Abstract
No abstract availableThis publication has 24 references indexed in Scilit:
- Type I procollagen: The gene‐protein system that harbors most of the mutations causing osteogenesis imperfecta and probably more common heritable disorders of connective tissueAmerican Journal of Medical Genetics, 1989
- Osteogenesis Imperfecta: The Molecular Basis of Clinical HeterogeneityaAnnals of the New York Academy of Sciences, 1988
- A synthetic model of collagen: An experimental investigation of the triple‐helix stabilityBiopolymers, 1988
- The A and B fragments of normal type I procollagen have a similar thermal stability to proteinase digestion but are selectively destabilized by structural mutationsEuropean Journal of Biochemistry, 1987
- Influence of different tripeptides on the stability of the collagen triple helix. I. Analysis of the collagen sequence and identification of typical tripeptidesBiopolymers, 1986
- Enzymatic Amplification of β-Globin Genomic Sequences and Restriction Site Analysis for Diagnosis of Sickle Cell AnemiaScience, 1985
- Nucleotide sequences of complementary deoxyribonucleic acids for the pro.alpha.1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolutionBiochemistry, 1983
- Triple helix–coil transition of covalently bridged collagenlike peptidesBiopolymers, 1980
- Chain conformation in the collagen moleculeJournal of Molecular Biology, 1979
- The role of polar and hydrophobic interactions for the molecular packing of type I collagen: A three-dimensional evaluation of the amino acid sequenceJournal of Molecular Biology, 1978