NMR Analysis of Partially-Folded States and Persistent Structure in the Alpha Subunit of Tryptophan Synthase: Implications for the Equilibrium Folding Mechanism of a 29 kDa TIM Barrel Protein

Antzeko izenburuak

• Partial NMR assignments and secondary structure mapping of the isolated α subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel protein
  nork: Vadrevu, Ramakrishna, et al.
  Argitaratua: (2003)
• A tightly-packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel protein
  nork: Wu, Ying, et al.
  Argitaratua: (2006)
• Long-range side-chain–main-chain interactions play crucial roles in stabilizing the (βα)(8) barrel motif of the alpha subunit of tryptophan synthase
  nork: Yang, Xiaoyan, et al.
  Argitaratua: (2007)
• 3D domain swapping in the TIM barrel of the α subunit of Streptococcus pneumoniae tryptophan synthase
  nork: Michalska, Karolina, et al.
  Argitaratua: (2020)
• The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.
  nork: Gualfetti, P. J., et al.
  Argitaratua: (1999)