Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: Description of the folding pathway

• DOI: 10.1073/pnas.94.25.13409
• Publication Date: 2002-07-26T14:40:52Z
• Authors: Chris J. Bond; Kam-Bo Wong; Jane Clarke; Alan R. Fersht; Valerie Daggett
• Keywords: Barnase; Folding (DSP implementation)

Residual structure in the denatured state of a protein may contain clues about early events folding. We have simulated by molecular dynamics barnase, which has been studied NMR spectroscopy. An ensemble 10 4 structures was generated after 2 ns unfolding and following for further ns. The heterogeneous, but there nonrandom, residual with persistent interactions. Helical C-terminal portion helix α1 (residues 13–17) α2 as well turn nonnative hydrophobic clustering between β3 β4 were observed, consistent data. In addition, tertiary contacts residues β-sheet. allow rudimentary data to be fleshed out. consistency simulation experiment inspires confidence methods. A description folding pathway barnase from native can constructed combining experimental φ value analysis NMR.