A folding pathway for betapep-4 peptide 33mer: from unfolded monomers and beta-sheet sandwich dimers to well-structured tetramers.

Lignende værker

• Folding of beta pep-4 beta-sheet sandwich dimers and tetramers is influenced by aliphatic hydrophobic residues at the intersubunit interface.
  af: Cox, A, et al.
  Udgivet: (2001)
• Folding and Unfolding of γTIM Monomers and Dimers
  af: Patel, Brijesh, et al.
  Udgivet: (2007)
• Muscle myosins form folded monomers, dimers, and tetramers during filament polymerization in vitro
  af: Liu, Xiong, et al.
  Udgivet: (2020)
• Solvation in protein (un)folding of melittin tetramer–monomer transition
  af: Othon, Christina M., et al.
  Udgivet: (2009)
• Multiple native-like conformations trapped via self-association-induced hydrophobic collapse of the 33-residue beta-sheet domain from platelet factor 4.
  af: Ilyina, E, et al.
  Udgivet: (1995)