Conclusions
The combination of experimental NMR techniques and of advanced MD
simulation allowed us to characterize the denatured state of a complex
protein as the HIV-1 protease under native conditions. This state
displays transient native and non-native secondary and tertiary
structures which could be of key relevance for guidance through the
complex folding process. The strategy we used for HIV-1 protease can be
easily applied to other proteins of comparable length.