Solid State NMR Reveals a pH-dependent Antiparallel β-Sheet Registry in Fibrils Formed by a β-Amyloid Peptide
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Gerd Buntkowsky | Richard D. Leapman | Fred Dyda | R. Leapman | F. Dyda | R. Tycko | G. Buntkowsky | W. Yau | A. Petkova | Robert Tycko | Aneta T. Petkova | Wai-Ming Yau | Wai‐Ming Yau
[1] L. Regan,et al. Guidelines for Protein Design: The Energetics of β Sheet Side Chain Interactions , 1995, Science.
[2] V. Conticello,et al. Exploiting amyloid fibril lamination for nanotube self-assembly. , 2003, Journal of the American Chemical Society.
[3] D. Filippov,et al. Secondary chemical shifts in immobilized peptides and proteins: A qualitative basis for structure refinement under Magic Angle Spinning , 2001, Journal of biomolecular NMR.
[4] R. Leapman,et al. Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. , 2002, Biochemistry.
[5] L. Serpell,et al. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. , 1997, Journal of molecular biology.
[6] P E Fraser,et al. Structure of beta-crystallite assemblies formed by Alzheimer beta-amyloid protein analogues: analysis by x-ray diffraction. , 1993, Biophysical journal.
[7] U Aebi,et al. Polymorphic fibrillar assembly of human amylin. , 1997, Journal of structural biology.
[8] J M Sturtevant,et al. Sidechain interactions in parallel beta sheets: the energetics of cross-strand pairings. , 1999, Structure.
[9] T. Benzinger,et al. Two-Dimensional Structure of β-Amyloid(10−35) Fibrils† , 2000 .
[10] A. Bax,et al. Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts , 1991 .
[11] J. Thornton,et al. Determinants of strand register in antiparallel β‐sheets of proteins , 1998, Protein science : a publication of the Protein Society.
[12] R. Tycko,et al. Sensitivity enhancement in structural measurements by solid state NMR through pulsed spin locking. , 2002, Journal of magnetic resonance.
[13] J. M. Smith,et al. Direct visualisation of the beta-sheet structure of synthetic Alzheimer's amyloid. , 2000, Journal of molecular biology.
[14] Eric J. Simon,et al. Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide , 1995, Nature Structural Biology.
[15] J. Thornton,et al. Prediction of strand pairing in antiparallel and parallel β‐sheets using information theory , 2002, Proteins.
[16] E. Oldfield,et al. Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach. , 1993, Science.
[17] Robert G Griffin,et al. Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[18] L. Tjernberg,et al. Assembling amyloid fibrils from designed structures containing a significant amyloid beta-peptide fragment. , 2002, The Biochemical journal.
[19] L. Serpell,et al. Structure and texture of fibrous crystals formed by Alzheimer's abeta(11-25) peptide fragment. , 2003, Structure.
[20] A. Zvi,et al. Solid–state NMR evidence for an antibody–dependent conformation of the V3 loop of HIV–1 gp120 , 1999, Nature Structural Biology.
[21] D. M. Morgan,et al. Structure of the β-Amyloid(10-35) Fibril , 2000 .
[22] J. J. Balbach,et al. Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance , 2002 .
[23] J. J. Balbach,et al. Increasing the amphiphilicity of an amyloidogenic peptide changes the beta-sheet structure in the fibrils from antiparallel to parallel. , 2004, Biophysical journal.
[24] Christopher M. Dobson,et al. The protofilament structure of insulin amyloid fibrils , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[25] Y. Ishii. 13C-13C dipolar recoupling under very fast magic angle spinning in solid-state nuclear magnetic resonance: Applications to distance measurements, spectral assignments, and high-throughput secondary-structure determination , 2001 .
[26] A. Bax,et al. Protein backbone angle restraints from searching a database for chemical shift and sequence homology , 1999, Journal of biomolecular NMR.
[27] Hazime Saitô,et al. Conformation‐dependent 13C chemical shifts: A new means of conformational characterization as obtained by high‐resolution solid‐state 13C NMR , 1986 .
[28] Y. Ishii,et al. Measurement of dipole-coupled lineshapes in a many-spin system by constant-time two-dimensional solid state NMR with high-speed magic-angle spinning , 2001 .
[29] D. Kirschner,et al. Structural analysis of Alzheimer's beta(1-40) amyloid: protofilament assembly of tubular fibrils. , 1998, Biophysical journal.
[30] S. Müller,et al. Studies on the in Vitro Assembly of Aβ 1–40: Implications for the Search for Aβ Fibril Formation Inhibitors , 2000 .
[31] C. Blake,et al. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation , 1998, Quarterly Reviews of Biophysics.
[32] R. Hodges,et al. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects , 1995, Journal of biomolecular NMR.
[33] Yoshitaka Ishii,et al. Constraints on supramolecular structure in amyloid fibrils from two-dimensional solid-state NMR spectroscopy with uniform isotopic labeling. , 2003, Journal of the American Chemical Society.
[34] L. Serpell,et al. Molecular Structure of a Fibrillar Alzheimer's Aβ Fragment† , 2000 .
[35] J T Finch,et al. Amyloid fibers are water-filled nanotubes , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[36] M. Billeter,et al. MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.
[37] Mitsuo Iwadate,et al. Cα and Cβ Carbon-13 Chemical Shifts in Proteins From an Empirical Database , 1999 .
[38] R. Leapman,et al. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[39] Elena Orlova,et al. Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing , 1999, The EMBO journal.
[40] T. Benzinger,et al. Propagating structure of Alzheimer’s β-amyloid(10–35) is parallel β-sheet with residues in exact register , 1998 .
[41] R. Leapman,et al. Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR† , 2000 .
[42] M. A. Wouters,et al. An analysis of side chain interactions and pair correlations within antiparallel β‐sheets: The differences between backbone hydrogen‐bonded and non‐hydrogen‐bonded residue pairs , 1995, Proteins.
[43] R. Leapman,et al. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils , 2000 .
[44] F. Dahlquist,et al. The carbonyl 13C chemical shift tensors of five peptides determined from 15N dipole-coupled chemical shift powder patterns , 1987 .
[45] M. Baldus,et al. Structural constraints from proton-mediated rare-spin correlation spectroscopy in rotating solids. , 2002, Journal of the American Chemical Society.
[46] R. Tycko. Insights into the amyloid folding problem from solid-state NMR. , 2003, Biochemistry.
[47] Q. Teng,et al. Determination of the carbon-13 chemical shift and nitrogen-14 electric field gradient tensor orientations with respect to the molecular frame in a polypeptide , 1992 .
[48] Robert C. Anderson,et al. Conformation of [1-13C,15N]Acetyl-L-carnitine. Rotational-Echo, Double-Resonance Nuclear Magnetic Resonance Spectroscopy , 1995 .
[49] T. Gullion,et al. Rotational-Echo, Double-Resonance NMR , 1989 .