Solid-state NMR studies of the prion protein H1 fragment

Protein Science

Volumn 5, Issue 8, 1996, Pages 1655-1661

  Heller, Jonathan ^a   Kolbert, Andrew C ^a,b,d   Larsen, Russell ^a,c,e   Ernst, Matthias ^a   Bekker, Tatiana ^b   Baldwin, Michael ^b   Prusiner, Stanley B ^b   Pines, Alexander ^a,c   Wemmer, David E ^a,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^d Lion Copolymer LLC   (United States)

^e E11 SSH   (United States)

Author keywords

chemical shift; prion peptides; rotational resonance; secondary structure; solid state NMR

Indexed keywords

ARTICLE; CONFORMATIONAL TRANSITION; HUMAN; NUCLEAR MAGNETIC RESONANCE; PATHOGENESIS; PRION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DETERMINATION; PROTEIN SECONDARY STRUCTURE; STRUCTURE ANALYSIS;

CRICETINAE; MESOCRICETUS AURATUS;

EID: 0030035952     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050819     Document Type: Article

References (53)

1. Borchelt DR, Scott M, Taraboulos A, Stahl N, Prusiner SB. 1990. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J Cell Biol 110:743-752.
2. Braunschweiler BL, Ernst RR. 1983. Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J Magn Reson 53: 521-528.
3. Bueler H, Aguzzi A, Sailer A, Greiner RA, Auenried P, Aguet M, Weissmann C. 1993. Mice devoid of PrP are resistant to scrapie. Cell 73:1339-1347.
4. Bueler H, Fisher M, Lang Y, Bluethmann H, Lipp HP, DeArmond SJ, Prusiner SB, Aguet M, Weissmann C. 1992. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356:577-582.
5. Caughey BW, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS. 1991. Secondary structure analysis of the scrapie-associated protein PrP27-30 in water by infrared spectroscopy. Biochemistry 30:7672-7680.
6. Cohen FE, Pan KM, Huang Z, Baldwin M, Fletterick RJ, Prusiner SB. 1994. Structural clues to prion replication. Science 264:530-531.
7. Creuzet F, McDermott A, Gebhard R, van der Hoef K, Spijker-Assink B, Herzfeld J, Lugtenburg J, Levitt MH, Griffin RG. 1991. Determination of membrane protein structure by rotational resonance NMR: Bacteriorhodopsin. Science 251:783-786.
8. 1H NMR spectra via two-dimensional homonuclear Hartmann-Hahn spectroscopy. J Am Chem Soc 107:2820.
9. de Dios AC, Pearson JG, Oldfield E. 1993. Secondary and tertiary structural effects on protein NMR chemical shifts: An ab initio approach. Science 260:1491-1496.
10. Gasset M, Baldwin MA, Lloyd D, Gabriel JM, Holtzman DM, Cohen F, Gletterick R, Prusiner SB. 1992. Predicted α-helical regions of the prion protein when synthesized as peptides form amyloid. Proc Natl Acad Sci USA 89:10940-10944.
11. Gullion T, Schaefer J. 1989. Rotational-echo double-resonance NMR. J Magn Reson 81:196-200.
12. Heller J, Larsen R, Ernst M, Kolbert A, Baldwin M, Prusiner SB, Wemmer DE, Pines A. 1996. Application of rotational resonance to inhomogeneously broadened systems. Chem Phys Lett 251:223-229.
13. Hsiao KK, Groth D, Scott M, Yang SL, Serban H, Rapp D, Foster D, Torchia M, DeArmond SJ, Prusiner SB. 1994. Serial transmission in rodents of neurodegeneration from transgenic mice expressing mutant prion protein. Proc Natl Acad Sci USA 91:9126-9130.
14. Hsiao KK, Scott M, Foster D, Groth DF, DeArmond SJ, Prusiner SB. 1990. Spontaneous neurodegeneration in transgenic mice with mutant prion protein. Science 250:1587-1590.
15. Huang Z, Gabriel JM, Baldwin MA, Fletterick RJ, Prusiner SB, Cohen FE. 1994. Proposed three dimensional structure for the cellular prion protein. Proc Natl Acad Sci USA 91:7139-7143.
16. Huang Z, Prusiner SB, Cohen FE. 1996. Scrapie prions: A three-dimensional model of an infectious fragment. Folding & Design 1:13-19.
17. Ishii Y, Terao T. 1995. Determination of interheteronuclear distances by observation of the Pake-doublet patterns using the MLEV-8 sequences with composite pulses. J Magn Resort A 115:116-118.
18. Jeener J, Meier BH, Bachman P, Ernst RR. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J Chem Phys 71: 4546-4553.
19. Kellings K, Meyer N, Mirenda C, Prusiner SB, Riesner D. 1992. Further analysis of nucleic acids in purified scrapie prion preparations by improved return refocussing gel electrophoresis (RRGE). J Gen Virol 73:1025-1029.
20. 13C NMR cross polarization/magic angle spinning spectroscopic characterization of solid polypeptides. Macromolecules 16:615-623.
21. Kubo A, McDowell CA. 1988. Spectral spin diffusion in polycrystalline solids under magic-angle spinning. J Chem Soc Faraday Trans 1 84:3713-3730.
22. Lansbury PTJ, Costa PR, Griffiths JM, Simon EJ, Auger M, Halverson KJ, Kocisko DA, Hendsch ZS, Ashburn TT, Spencer RGS, Tidor B, Griffin RG. 1995. Structural model for the β amyloid fibril: Interstrand alignment of an antiparallel β sheet comprising a C-terminal peptide. Nature Structural Biol 2:990-998.
23. Levante TO, Baldus M, Meier BH, Ernst RR. 1995. Formalized quantum mechanical Floquet theory and its application to sample spinning in nuclear magnetic resonance. Mol Phys 86:1195-1212.
24. Levitt MH, Raleigh DP, Creuzet R, Griffin RG. 1990. Theory and simulations of homonuclear spin pair systems in rotating solids. J Chem Phys 92:6347-6364.
25. McKinley MP, Meyer RK, Kenaga L, Rahbar F, Cotter R, Serban A, Prusiner SB. 1991. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J Virol 65:1440-1449.
26. Meyer N, Rosenbaum V, Schmidt B, Gilles K, Mirenda C, Groth D, Prusiner SB. 1991. Search for a putative scrapie genome in purified prion fractions reveals a paucity of nucleic acids. J Gen Virol 72:37-49.
27. Morris GA, Freeman R. 1978. Selective excitation in Fourier transform nuclear magnetic resonance. J Magn Reson 29:433-462.
28. Nguyen JT, Baldwin MA, Cohen FE, Prusiner SB. 1995a. Prion Protein Peptides Induce α-helix to β-sheet conformational transitions. Biochemistry 34:4186-4192.
29. Nguyen JT, Inouye H, Baldwin MA, Fletterick RJ, Cohen FE, Prusiner SB, Kirschner DA. 1995b. X-ray diffraction of scrapie prion rods and PrP peptides. J Mol Biol 252:412-422.
30. Pan KM, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, Mehlhorn I, Huang Z, Fletterick RJ, Cohen FE, Prusiner SB. 1993. Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90:10962-10966.
31. Peerson O, Groesbeek M, Aimoto S, Smith SO. 1995. Analysis of rotational resonance magnetization exchange curves of crystalline peptides. J Am Chem Soc 117:7228-7237.
32. Pines A, Gibby MG, Waugh JS. 1973. Proton-enhanced NMR of dilute spins in solids. J Chem Phys 59:569-590.
33. Prusiner SB. 1992. Chemistry and biology of prions. Biochemistry 31:12277-12288.
34. Prusiner SB, Groth D, Serban A, Koehler R, Foster D, Torchia M, Burton D, Yang SL, DeArmond SJ. 1993. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP anti-bodies. Proc Natl Acad Sci USA 90:10608-10612.
35. Prusiner SB, McKinley MP, Bowman KA, Bolton DC, Bendheim PE, Groth DF, Glenner GG. 1983. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35:349-358.
36. Raleigh DP, Creuzet F, Das Gupta SK, Levitt MH, Griffin RG. 1989. Measurement of internuclear distances in polycrystalline solids: Rotationally enhanced transfer of spin magnetization. J Am Chem Soc 111:4502-4503.
37. Raleigh DP, Levitt MH, Griffin RG. 1988. Rotational resonance in solid state NMR. Chem Phys Lett 146:71-76.
38. Safar J, Roller PP, Gajdusek DC, Gibbs CJJ. 1994. Scrapie amyloid (prion) protein has the conformational characteristics of an aggregated molten globule folding intermediate. Biochemistry 33:8375-8383.
39. 13C NMR. Magn Reson Chem 24:835-852.
40. Schaefer J, Stejskal EO. 1976. Carbon-13 nuclear magnetic resonance of polymers spinning at the magic angle. J Am Chem Soc 98:1031-1032.
41. Shirley JH. 1965. Solution of the Schödinger equation with a Hamiltonian periodic in time. Phys Rev B 138:979.
42. Smith SA, Levante TO, Meier BH, Ernst RR. 1994a. Computer simulations in magnetic resonance - An object-oriented programming approach. J Magn Reson A 106:75-105.
43. Smith SO, Jonas R, Braiman M, Bormann BJ. 1994b. Structure and orientation of the transmembrane domain of glycophorin A in lipid bilayers. Biochemistry 33:6334-6341.
44. 13C nuclear magnetic resonance chemical shifts. J Am Chem Soc 113:5490-5492.
45. Stahl N, Baldwin MA, Teplow DB, Hood L, Gibson BW, Burlingame AL, Prusiner SB. 1993. Structural analysis of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32:1991-2002.
46. Stahl N, Borchelt DR, Hsiao K, Prusiner SB. 1987. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51:229-240.
47. Taraboulos A, Serban D, Prusiner SB. 1990. Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells. J Cell Biol 110:2117-2132.
48. Thompson LK, McDermott A, Raap J, van der Wielen CM, Lugtenburg J, Herzfeld J, Griffin RG. 1992. NMR study of active site structure in bR: Conformation of schiff base linkage. Biochemisiry 31:7931-7938.
49. Tomita Y, O'Connor EJ, McDermott A. 1994. A method for dihedral angle measurement in solids: Rotational resonance NMR of a transition-state inhibitor of triose phosphate isomerase. J Am Chem Soc 116: 8766-8771.
50. Tycko R, Dabbagh G. 1990. Measurement of nuclear magnetic dipole-dipole couplings in magic angle spinning NMR. Chem Phys Lett 173:461 -465.
51. Vega S. 1992. The Floquet theory of nuclear magnetic resonance spectroscopy of single spins and dipolar coupled spin pairs in rotating solids. J Chem Phys 96:2655-2680.
52. 13C chemical shift data. J Biomol NMR 4:171-180.
53. Zhang H, Kaneko K, Nguyen JT, Livshits TL, Baldwin MA, Cohen FE, James TL, Prusiner SB. 1995. Conformational transitions in peptides containing two putative α-hehces of the prion protein. J Mol Biol 250: 514-526.