Journal
JOURNAL OF PHYSICAL CHEMISTRY B
Volume 115, Issue 28, Pages 8910-8924Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jp200790h
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Funding
- Czech Science Foundation [203/08/0114]
- Czech Ministry of Education [LC 512]
- Academy of Sciences (Praemium Academie)
- International Max Planck Research School
- University of Leeds
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Using a combination of experimental techniques (circular dichroism, differential scanning calorimetry, and NMR) and molecular dynamics simulations, we performed an extensive study of denaturation of the Trp-cage miniprotein by urea and guanidinium. The experiments, despite their different sensitivities to various aspects of the denaturation process, consistently point to simple, two-state unfolding process. Microsecond molecular dynamics simulations with a femto-second time resolution allow us to unravel the detailed molecular mechanism of Trp-cage unfolding. The process starts with a destabilizing proline shift in the hydrophobic core of the miniprotein, followed by a gradual destruction of the hydrophobic loop and the a-helix. Despite differences in interactions of urea vs guanidinium with various peptide moieties, the overall destabilizing action of these two denaturants on Trp-cage is very similar.
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