  We report the results of molecular dynamics simulations of an off-lattice
protein model featuring a physical force-field and amino-acid sequence. We show
that localized modes of nonlinear origin (discrete breathers) emerge naturally
as continuations of a subset of high-frequency normal modes residing at
specific sites dictated by the native fold. In the case of the small
$\beta$-barrel structure that we consider, localization occurs on the turns
connecting the strands. At high energies, discrete breathers stabilize the
structure by concentrating energy on few sites, while their collapse marks the
onset of large-amplitude fluctuations of the protein. Furthermore, we show how
breathers develop as energy-accumulating centres following perturbations even
at distant locations, thus mediating efficient and irreversible energy
transfers. Remarkably, due to the presence of angular potentials, the breather
induces a local static distortion of the native fold. Altogether, the
combination of this two nonlinear effects may provide a ready means for
remotely controlling local conformational changes in proteins.
