000080946 001__ 80946
000080946 005__ 20180317094759.0
000080946 02470 $$2ISI$$a000223713801608
000080946 037__ $$aCONF
000080946 245__ $$aStructure and stability of copper-prion protein
000080946 269__ $$a2004
000080946 260__ $$c2004
000080946 336__ $$aConference Papers
000080946 520__ $$aRecent EPR-measurements on the mouse prion protein (mPrP) have indicated that the structured C-terminal domain is capable of binding Cu(II) with high affinity. The structure of Cu(II) binding sites in PrPc are unravelled by exploiting mixed quantum-classical Car-Parrinello simulations and by computing EPR hyperfine consts. for the paramagnetic Cu(II) center. The putative binding sites, once validated by comparing with the exptl. EPR parameters, provide detailed information concerning the Cu(II) localization and coordination. The influence of Cu(II) binding sites on the structural stability of the cellular form (PrPc) and its conversion to the scrapie form (PrPsc) is investigated. [on SciFinder (R)]
000080946 700__ $$0241547$$aColombo, Maria C.$$g154447
000080946 700__ $$aVandeVondele, Joost H. B.
000080946 700__ $$aLaio, Alesandro
000080946 700__ $$0241546$$aGuidoni, Leonardo$$g153494
000080946 700__ $$0241350$$aRothlisberger, Ursula$$g150117
000080946 773__ $$qPHYS-661$$tAbstracts of Papers, 228th ACS National Meeting, Philadelphia, PA, United States, August 22-26, 2004
000080946 909CO $$ooai:infoscience.tind.io:80946$$pSB$$pconf
000080946 909C0 $$0252093$$pLCBC$$xU2
000080946 937__ $$aLCBC-CONF-2004-005
000080946 970__ $$a99/LCBC
000080946 973__ $$aEPFL$$rREVIEWED$$sPUBLISHED
000080946 980__ $$aCONF