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Research Paper

Thermodynamic characterization for the denatured state of bovine prion protein and the BSE Associated variant E211K

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Pages 301-309 | Received 19 Jun 2018, Accepted 03 Oct 2018, Published online: 24 Oct 2018

References

  • Prusiner SB. Prions. Proc Natl Acad Sci USA. 1998;95:13363–13383.
  • Collinge J. Prion diseases of humans and animals: their causes and molecular basis. Annu Rev Neurosci. 2001;24:519–550.
  • Caughey B, Chesebro B. Transmissible spongiform encephalopathies and prion protein interconversions. Adv Virus Res. 2001;56:277–311.
  • Weissmann C. The ninth datta lecture. molecular biology of transmissible spongiform encephalopathies. FEBS Lett. 1996;389:3–11.
  • Lopez Garcia F, Zahn R, Riek R, et al. NMR structure of the bovine prion protein. Proc Natl Acad Sci USA. 2000;97:8334–8339.
  • Hornemann S, Schorn C, Wuthrich K. NMR structure of the bovine prion protein isolated from healthy calf brains. EMBO Rep. 2004;5:1159–1164.
  • Cho JH, Raleigh DP. Experimental characterization of the denatured state ensemble of proteins. Methods Mol Biol. 2009;490:339–351.
  • Yao J, Chung J, Eliezer D, et al. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry. 2001;40:3561–3571.
  • Wright PE, Dyson HJ, Lerner RA. Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. Biochemistry. 1988;27:7167–7175.
  • Freund SM, Wong KB, Fersht AR. Initiation sites of protein folding by NMR analysis. Proc Natl Acad Sci U S. 1996;93:10600–10603.
  • Blanco FJ, Serrano L, Forman-Kay JD. High populations of non-native structures in the denatured state are compatible with the formation of the native folded state. J Mol Biol. 1998;284:1153–1164.
  • Kortemme T, Kelly MJ, Kay LE, et al. Similarities between the spectrin SH3 domain denatured state and its folding transition state. J Mol Biol. 2000;297:1217–1229.
  • Radford SE, Dobson CM. From computer simulations to human disease: emerging themes in protein folding. Cell. 1999;97:291–298.
  • Thirumalai D, Klimov DK. Fishing for folding nuclei in lattice models and proteins. Fold Des. 1998;3: R112–R118. discussion R107.
  • Myers JK, Pace CN, Scholtz JM. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 1995;4:2138–2148.
  • Robertson AD, Murphy KP. Protein structure and the energetics of protein stability. Chem Rev. 1997;97:1251–1268.
  • Hsiao K, Meiner Z, Kahana E, et al. Mutation of the prion protein in Libyan Jews with Creutzfeldt-Jakob disease. N Engl J Med. 1991;324:1091–1097.
  • Zhang Y, Swietnicki W, Zagorski MG, et al. Solution structure of the E200K variant of human prion protein. Implications for the mechanism of pathogenesis in familial prion diseases. J Biol Chem. 2000;275:33650–33654.
  • Greene RF Jr., Pace CN. Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin. J Biol Chem. 1974;249:5388–5393.
  • Becktel WJ, Schellman JA. Protein stability curves. Biopolymers. 1987;26:1859–1877.
  • Swietnicki W, Petersen RB, Gambetti P, et al. Familial mutations and the thermodynamic stability of the recombinant human prion protein. J Biol Chem. 1998;273:31048–31052.
  • Apetri AC, Maki K, Roder H, et al. Early intermediate in human prion protein folding as evidenced by ultrarapid mixing experiments. J Am Chem Soc. 2006;128:11673–11678.
  • Honda RP, Xu M, Yamaguchi KI, et al. A native-like intermediate serves as a branching point between the folding and aggregation pathways of the mouse prion protein. Structure. 2015;23:1735–1742.
  • Honda RP, Yamaguchi K, Kuwata K. Acid-induced molten globule state of a prion protein: crucial role of Strand 1-Helix 1-Strand 2 segment. J Biol Chem. 2014;289:30355–30363.
  • Nicholson EM, Mo H, Prusiner SB, et al. Differences between the prion protein and its homolog Doppel: a partially structured state with implications for scrapie formation. J Mol Biol. 2002;316:807–815.
  • Moulick R, Udgaonkar JB. Thermodynamic characterization of the unfolding of the prion protein. Biophys J. 2014;106:410–420.
  • Canello T, Friedman-Levi Y, Mizrahi M, et al. Copper is toxic to PrP-ablated mice and exacerbates disease in a mouse model of E200K genetic prion disease. Neurobiol Dis. 2012;45:1010–1017.
  • Rosenmann H, Halimi M, Kahana I, et al. Differential allelic expression of PrP mRNA in carriers of the E200K mutation. Neurology. 1997;49:851–856.
  • Vrentas CE, Greenlee JJ, Foster GH, et al. Effects of a naturally occurring amino acid substitution in bovine PrP: a model for inherited prion disease in a natural host species. BMC Res Notes. 2017;10:759.
  • Vrentas CE, Onstot S, Nicholson EM. A comparative analysis of rapid methods for purification and refolding of recombinant bovine prion protein. Protein Expr Purif. 2012;82:380–388.
  • Santoro MM, Bolen DW. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants. Biochemistry. 1988;27:8063–8068.
  • Pace CN. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 1986;131:266–280.
  • Swint L, Robertson AD. Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation. Protein Sci. 1993;2:2037–2049.
  • Fu H, Grimsley G, Scholtz JM, et al. Increasing protein stability: importance of DeltaC(p) and the denatured state. Protein Sci. 2010;19:1044–1052.