Computational Studies of the Structural Stability of Rabbit Prion Protein Compared to Human and Mouse Prion Proteins

Physics – Biological Physics

Scientific paper

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

Contributed as an invited Book Chapter to "Neurodegenerative Diseases / Book 2, Raymond Chuen-Chung Chang (eds.), INTECH Open

Scientific paper

Prion diseases are invariably fatal and highly infectious neurodegenerative diseases affecting humans and animals. The neurodegenerative diseases such as Creutzfeldt-Jakob disease, variant Creutzfeldt-Jakob diseases, Gerstmann-Str$\ddot{a}$ussler-Scheinker syndrome, Fatal Familial Insomnia, Kuru in humans, scrapie in sheep, bovine spongiform encephalopathy (or 'mad-cow' disease) and chronic wasting disease in cattle belong to prion diseases. By now there have not been some effective therapeutic approaches to treat all these prion diseases. Dogs, rabbits and horses were reported to be resistant to prion diseases. By the end of year 2010 all the NMR structures of dog, rabbit and horse prion proteins (X-ray for rabbits too) had been finished to release into protein data bank. Thus, at this moment it is very worth studying the NMR and X-ray molecular structures of horse, dog and rabbit prion proteins to obtain insights into their immunity prion diseases. The author found that dog and horse prion proteins have stable molecular dynamical structures whether under neutral or low pH environments, but rabbit prion protein has stable molecular dynamical structures only under neutral pH environment. Under low pH environment, the stable $\alpha$-helical molecular structures of rabbit prion protein collapse into $\beta$-sheet structures. This article focuses the studies on rabbit prion protein (within its C-terminal NMR, Homology and X-ray molecular structured region RaPrP$^\text{C}$ (120-230)), compared with human and mouse prion proteins (HuPrP$^\text{C}$ (125-228) and MoPrP$^\text{C}$ (124-226) respectively). The author finds that some salt bridges contribute to the structural stability of rabbit prion protein under neutral pH environment.

No associations

LandOfFree

Say what you really think

Search LandOfFree.com for scientists and scientific papers. Rate them and share your experience with other people.

Rating

Computational Studies of the Structural Stability of Rabbit Prion Protein Compared to Human and Mouse Prion Proteins does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Computational Studies of the Structural Stability of Rabbit Prion Protein Compared to Human and Mouse Prion Proteins, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Computational Studies of the Structural Stability of Rabbit Prion Protein Compared to Human and Mouse Prion Proteins will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFWR-SCP-O-571731

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.