NMR Conformational and Dynamic Consequences of a Gly to Ser Substitution in an Osteogenesis Imperfecta Collagen Model Peptide

Similar Items

• Osteogenesis Imperfecta Model Peptides: Incorporation of Residues Replacing Gly within a Triple Helix Achieved by Renucleation and Local Flexibility
  od: Xiao, Jianxi, i dr.
  Izdano: (2011)
• Osteogenesis Imperfecta Missense Mutations in Collagen: Structural consequences of a glycine to alanine replacement at a highly charged site
  od: Xiao, Jianxi, i dr.
  Izdano: (2011)
• Sequence Environment of Mutation Affects Stability and Folding in Collagen Model Peptides of Osteogenesis Imperfecta
  od: Bryan, Michael A., i dr.
  Izdano: (2011)
• Recombinant Collagen Studies Link the Severe Conformational Changes Induced by Osteogenesis Imperfecta Mutations to the Disruption of a Set of Interchain Salt Bridges
  od: Xu, Ke, i dr.
  Izdano: (2008)
• Destabilization of osteogenesis imperfecta collagen-like model peptides correlates with the identity of the residue replacing glycine
  od: Beck, Konrad, i dr.
  Izdano: (2000)