Identifying the structural boundaries of independent folding domains in the alpha subunit of tryptophan synthase, a beta/alpha barrel protein.

פריטים דומים

• The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.
  מאת: Gualfetti, P. J., et al.
  יצא לאור: (1999)
• 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
  מאת: Vadrevu, Ramakrishna, et al.
  יצא לאור: (2007)
• 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
  מאת: Wu, Ying, et al.
  יצא לאור: (2006)
• Characterisation of the tryptophan synthase alpha subunit in maize
  מאת: Kriechbaumer, Verena, et al.
  יצא לאור: (2008)
• Long-range side-chain–main-chain interactions play crucial roles in stabilizing the (βα)(8) barrel motif of the alpha subunit of tryptophan synthase
  מאת: Yang, Xiaoyan, et al.
  יצא לאור: (2007)