  Prion diseases are invariably fatal and highly infectious neurodegenerative
diseases that affect a wide variety of mammalian species such as sheep, goats,
mice, humans, chimpanzees, hamsters, cattle, elks, deer, minks, cats, chicken,
pigs, turtles, etc. These neurodegenerative diseases are caused by the
conversion from a soluble normal cellular protein into insoluble abnormally
folded infectious prions and the conversion is believed to involve
conformational change from a predominantly alpha-helical protein to one rich in
beta-sheet structure. Such conformational changes may be amenable to study by
molecular dynamics (MD) techniques. For rabbits, classical studies show they
have a low susceptibility to be infected, but in 2012 it was reported that
rabbit prion can be generated (though not directly) and the rabbit prion is
infectious and transmissible (Proceedings of the National Academy of Sciences
USA 109(13): 5080-5). This paper studies the NMR and X-ray molecular structures
of rabbit prion protein wild-type and mutants by MD techniques, in order to
understand the specific mechanism of rabbit prion protein and rabbit prions.
