  Prion diseases cover a large range of neurodegenerative diseases in humans
and animals, which are invariably fatal and highly infectious. By now there
have not been some effective therapeutic approaches or medications to treat all
prion diseases. Fortunately, numerous experimental experiences have showed that
rabbits are resistant to infection from prion diseases isolated from other
species, and recently the molecular structures of rabbit prion protein and its
mutants were released into protein data bank. Prion diseases are "protein
structural conformational" diseases. Thus, in order to reveal some secrets of
prion diseases, it is amenable to study rabbits by techniques of the molecular
structure and its dynamics. Wen et al. (PLoS One 5(10) e13273 (2010), Journal
of Biological Chemistry 285(41) 31682-31693 (2010)) reported the surface of NMR
RaPrPC(124-228) molecular snapshot has a large land of continuous positive
charge distribution, which contributes to the structural stability of rabbit
prion protein. This is just the property at one snapshot. This paper confirms a
large land of positive charge distribution has still been reserved during the
long molecular dynamics of 30 nanoseconds in many environments, but the
continuous of the land has not been always reserved yet. These results may be
useful for the medicinal treatment of prion diseases.
