Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2.

Documenti analoghi

• Sensitivity of the folding/unfolding transition state ensemble of chymotrypsin inhibitor 2 to changes in temperature and solvent
  di: Day, Ryan, et al.
  Pubblicazione: (2005)
• Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.
  di: Otzen, D E, et al.
  Pubblicazione: (1994)
• Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations
  di: Merchant, Kusai A., et al.
  Pubblicazione: (2007)
• The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding.
  di: de Prat Gay, G, et al.
  Pubblicazione: (1994)
• Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution
  di: Kazmirski, Steven L., et al.
  Pubblicazione: (2001)