Exploring the landscape of large scale conformational changes such as protein folding at
atomistic detail poses a considerable computational challenge. Coarse-grained …

Successful simulations of biomolecules require sufficient sampling of the relevant
conformational space. This has remained a major challenge due to large conformational …

We simulate the folding and fold switching of the C‐terminal domain (CTD) of the
transcription factor RfaH using an all‐atom physics‐based model augmented with a dual …

Proteins such as the transcription factor RfaH can change biological function by switching
between distinct three-dimensional folds. RfaH regulates transcription if the C-terminal …

Recent experiments suggest that an amino acid sequence encodes not only the native fold
of a protein but also other forms that are essential for its function or are important during …

We introduce Replica-Exchange-with-Tunneling (RET) simulations as a tool for studies of
the conversion between polymorphic amyloids. For the 11-residue amyloid-forming cylindrin …

We study wild type and mutants of the A and B domain of protein G using all-atom Go-
models. Our data substantiate the usefulness of such simulation for probing the folding …

Structure-based models are successful at conjugating the essence of the energy landscape
theory of protein folding with an easy and efficient implementation. Recently, their realm …

Protein collapse from a random chain to the native state involves a dynamical phase
transition. During the process, new scales and collective variables become excited while old …

Functional residues can modulate the folding mechanisms of proteins. In some proteins,
mutations to such residues can radically change the primary folding route. Is it possible then …