Related ArticlesPrion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR.
Fold Des. 1998;3(5):313-20
Authors: Sharman GJ, Kenward N, Williams HE, Landon M, Mayer RJ, Searle MS
BACKGROUND: Transmissible spongiform encephalopathies are a group of neurodegenerative disorders of man and animals that are believed to be caused by an alpha-helical to beta-sheet conformational change in the prion protein, PrP. Recently determined NMR structures of recombinant PrP (residues 121-231 and 90-231) have identified a short two-stranded anti-parallel beta sheet in the normal cellular form of the protein (PrPC). This beta sheet has been suggested to be involved in seeding the conformational transition to the disease-associated form (PrPSc) via a partially unfolded intermediate state. RESULTS: We describe CD and NMR studies of three peptides (125-170, 142-170 and 156-170) that span the beta-sheet and helix 1 region of PrP, forming a large part of the putative PrPSc-PrPC binding site that has been proposed to be important for self-seeding replication of PrPSc. The data suggest that all three peptides in water have predominantly helical propensities, which are enhanced in aqueous methanol (as judged by deviations from random-coil Halpha chemical shifts and 3JHalpha-NH values). Although the helical propensity is most marked in the region corresponding to helix 1 (144-154), it is also apparent for residues spanning the two beta-strand sequences. CONCLUSIONS: We have attempted to model the conformational properties of a partially unfolded state of PrP using peptide fragments spanning the region 125-170. We find no evidence in the sequence for any intrinsic conformational preference for the formation of extended beta-like structure that might be involved in promoting the PrPC-PrPSc conformational transition.
Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Density functional calculations of backbone 15N shielding tensors in beta-sheet and turn residues of protein G
Abstract We performed density functional calculations of backbone 15N shielding tensors in the regions of beta-sheet and turns of protein G. The calculations were carried out for all twenty-four beta-sheet residues and eight beta-turn residues in the protein GB3 and the results were compared with the available experimental data from solid-state and solution NMR measurements. Together with the alpha-helix data, our calculations cover 39 out of the 55 residues (or 71%) in GB3....
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[NMR paper] NMR assignment of the chicken prion protein fragments chPrP(128-242) and chPrP(25-242
NMR assignment of the chicken prion protein fragments chPrP(128-242) and chPrP(25-242).
Related Articles NMR assignment of the chicken prion protein fragments chPrP(128-242) and chPrP(25-242).
J Biomol NMR. 2004 Sep;30(1):97
Authors: Lysek DA, Calzolai L, Wüthrich K
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[NMR paper] Letters to the Editor: NMR assignment of the chicken prion protein fragments chPrP(12
Letters to the Editor: NMR assignment of the chicken prion protein fragments chPrP(128-242) and chPrP(25-242) / NMR assignment of the turtle prion protein fragment tPrP(121-225).
Letters to the Editor: NMR assignment of the chicken prion protein fragments chPrP(128-242) and chPrP(25-242) / NMR assignment of the turtle prion protein fragment tPrP(121-225).
J Biomol NMR. 2004 Sep;30(1):97
Authors:
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[NMR paper] CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in
CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
Related Articles CD and NMR studies of prion protein (PrP) helix 1. Novel implications for its role in the PrPC-->PrPSc conversion process.
J Biol Chem. 2003 Dec 12;278(50):50175-81
Authors: Ziegler J, Sticht H, Marx UC, Müller W, Rösch P, Schwarzinger S
The conversion of prion helix 1 from an alpha-helical into an extended conformation is generally assumed to be an essential step in the conversion of the cellular isoform...
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[NMR paper] Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
Related Articles Folding of a beta-sheet protein monitored by real-time NMR spectroscopy.
J Mol Biol. 2003 May 16;328(5):1161-71
Authors: Mizuguchi M, Kroon GJ, Wright PE, Dyson HJ
At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N...
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[NMR paper] Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational
Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational investigation of three-stranded antiparallel beta-sheet-forming peptides.
Related Articles Insights into the determinants of beta-sheet stability: 1H and 13C NMR conformational investigation of three-stranded antiparallel beta-sheet-forming peptides.
J Pept Res. 2003 Apr;61(4):177-88
Authors: Santiveri CM, Rico M, Jiménez MA, Pastor MT, Pérez-Payá E
In a previous study we designed a 20-residue peptide able to adopt a significant population of a three-stranded...
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[NMR paper] Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics
Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
Related Articles Comparison of protein backbone entropy and beta-sheet stability: NMR-derived dynamics of protein G B1 domain mutants.
J Am Chem Soc. 2001 Jan 10;123(1):185-6
Authors: Stone MJ, Gupta S, Snyder N, Regan L
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[NMR paper] High helicity of peptide fragments corresponding to beta-strand regions of beta-lacto
High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Related Articles High helicity of peptide fragments corresponding to beta-strand regions of beta-lactoglobulin observed by 2D-NMR spectroscopy.
Fold Des. 1996;1(4):255-63
Authors: Kuroda Y, Hamada D, Tanaka T, Goto Y
BACKGROUND: Whereas protein fragments, when they are structured, adopt conformations similar to that found in the native state, the high helical propensity of beta-lactoglobulin, a predominantly beta-sheet...
Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125
Linear Mode
