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

Ítems similars

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• Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.
  per: Otzen, D E, et al.
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• Characterizing the unfolded states of proteins using single-molecule FRET spectroscopy and molecular simulations
  per: Merchant, Kusai A., et al.
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• 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.
  per: de Prat Gay, G, et al.
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