The Homology Structure and Dynamics

Abstract

Vorberg et al. (J Virol 77(3):2003--2009, 2003) reported that multiple amino acid residues (such as N173, V214) within the rabbit prion protein inhibit formation of its abnormal isoform, but there was not any X-ray or NMR molecular structure of RaPrPCin Year 2003. Thus, in 2004 V.C. Epa of CSIRO made a rabbit prion protein homology structure modelrabbit homolgyfor RaPrPC(120--229) (denoted as 6EPA.pdb by this book) (Zhang JP, Varghese JN, Epa VC, Studies on the conformational stability of the rabbit prion protein. CSIRO Preventative Health National Research Flagship Science Retreat, Aitken Hill, Melbourne, 12--15 Sept 2006, Poster in Excellence). This chapter studies the MD of this homology modelhomology model. First we briefly introduce some basic knowledge about molecular modelingmolecular modeling.