메뉴 건너뛰기




Volumn 117, Issue 26, 2013, Pages 7918-7928

Local frustration determines molecular and macroscopic helix structures

Author keywords

[No Author keywords available]

Indexed keywords

MODELS; MORPHOLOGY;

EID: 84879751802     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp4040503     Document Type: Article
Times cited : (12)

References (39)
  • 1
    • 0030373310 scopus 로고    scopus 로고
    • Snelson on the Tensegrity Invention
    • Snelson, K. Snelson on the Tensegrity Invention Space Struct. 1996, 11, 43-48
    • (1996) Space Struct. , vol.11 , pp. 43-48
    • Snelson, K.1
  • 3
    • 77955204651 scopus 로고    scopus 로고
    • Self-Assembly of Three-Dimensional Prestressed Tensegrity Structures from DNA
    • Liedl, T.; Högberg, B.; Tytell, J.; Ingber, D. E.; Shih, W. M. Self-Assembly of Three-Dimensional Prestressed Tensegrity Structures from DNA Nat. Nanotechnol. 2010, 5, 520-4
    • (2010) Nat. Nanotechnol. , vol.5 , pp. 520-524
    • Liedl, T.1    Högberg, B.2    Tytell, J.3    Ingber, D.E.4    Shih, W.M.5
  • 4
    • 35349019738 scopus 로고    scopus 로고
    • Self-Assembly of Multidomain Peptides: Balancing Molecular Frustration Controls Conformation and Nanostructure
    • Dong, H.; Paramonov, S. E.; Aulisa, L.; Bakota, E. L.; Hartgerink, J. D. Self-Assembly of Multidomain Peptides: Balancing Molecular Frustration Controls Conformation and Nanostructure J. Am. Chem. Soc. 2007, 129, 12468-72
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12468-12472
    • Dong, H.1    Paramonov, S.E.2    Aulisa, L.3    Bakota, E.L.4    Hartgerink, J.D.5
  • 5
    • 12244249201 scopus 로고    scopus 로고
    • Self-Propagating, Molecular-Level Polymorphism in Alzheimer's Beta-Amyloid Fibrils
    • Petkova, A. T.; Leapman, R. D.; Guo, Z.; Yau, W.-M.; Mattson, M. P.; Tycko, R. Self-Propagating, Molecular-Level Polymorphism in Alzheimer's Beta-Amyloid Fibrils Science 2005, 307, 262-5
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.3    Yau, W.-M.4    Mattson, M.P.5    Tycko, R.6
  • 6
    • 33744831968 scopus 로고    scopus 로고
    • Polymorphic Fibril Formation by Residues 10-40 of the Alzheimer's Beta-Amyloid Peptide
    • Paravastu, A. K.; Petkova, A. T.; Tycko, R. Polymorphic Fibril Formation by Residues 10-40 of the Alzheimer's Beta-Amyloid Peptide Biophys. J. 2006, 90, 4618-29
    • (2006) Biophys. J. , vol.90 , pp. 4618-4629
    • Paravastu, A.K.1    Petkova, A.T.2    Tycko, R.3
  • 9
    • 80053151969 scopus 로고    scopus 로고
    • Geometry and Mechanics in the Opening of Chiral Seed Pods
    • Armon, S.; Efrati, E.; Kupferman, R.; Sharon, E. Geometry and Mechanics in the Opening of Chiral Seed Pods Science 2011, 333, 1726-30
    • (2011) Science , vol.333 , pp. 1726-1730
    • Armon, S.1    Efrati, E.2    Kupferman, R.3    Sharon, E.4
  • 11
    • 30344457011 scopus 로고    scopus 로고
    • Probing the Mechanism of Amyloidogenesis through a Tandem Repeat of the PI3-SH3 Domain Suggests a Generic Model for Protein Aggregation and Fibril Formation
    • Bader, R.; Bamford, R.; Zurdo, J.; Luisi, B. F.; Dobson, C. M. Probing the Mechanism of Amyloidogenesis through a Tandem Repeat of the PI3-SH3 Domain Suggests a Generic Model for Protein Aggregation and Fibril Formation J. Mol. Biol. 2006, 356, 189-208
    • (2006) J. Mol. Biol. , vol.356 , pp. 189-208
    • Bader, R.1    Bamford, R.2    Zurdo, J.3    Luisi, B.F.4    Dobson, C.M.5
  • 14
    • 77957324146 scopus 로고    scopus 로고
    • Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy
    • VanMelckebeke, H.; Wasmer, C.; Lange, A.; Ab, E.; Loquet, A.; Böckmann, A.; Meier, B. H. Atomic-Resolution Three-Dimensional Structure of HET-s(218-289) Amyloid Fibrils by Solid-State NMR Spectroscopy J. Am. Chem. Soc. 2010, 132, 13765-75
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 13765-13775
    • Vanmelckebeke, H.1    Wasmer, C.2    Lange, A.3    Ab, E.4    Loquet, A.5    Böckmann, A.6    Meier, B.H.7
  • 16
    • 18144408042 scopus 로고    scopus 로고
    • Helicoid to Spiral Ribbon Transition
    • Ghafouri, R.; Bruinsma, R. Helicoid to Spiral Ribbon Transition Phys. Rev. Lett. 2005, 94, 1-4
    • (2005) Phys. Rev. Lett. , vol.94 , pp. 1-4
    • Ghafouri, R.1    Bruinsma, R.2
  • 17
    • 77749262181 scopus 로고    scopus 로고
    • Generation of Ribbons, Helicoids, and Complex Scherk Surfaces in Laser-Matter Interactions
    • Lugomer, S.; Fukumoto, Y. Generation of Ribbons, Helicoids, and Complex Scherk Surfaces in Laser-Matter Interactions Phys. Rev. E 2010, 81, 1-11
    • (2010) Phys. Rev. e , vol.81 , pp. 1-11
    • Lugomer, S.1    Fukumoto, Y.2
  • 18
    • 0035981012 scopus 로고    scopus 로고
    • Tension-Induced Straightening Transition of Self-Assembled Helical Ribbons
    • Smith, B.; Zastavker, Y. V.; Benedek, G. B. Tension-Induced Straightening Transition of Self-Assembled Helical Ribbons Phys. Rev. Lett. 2001, 87, 26-29
    • (2001) Phys. Rev. Lett. , vol.87 , pp. 26-29
    • Smith, B.1    Zastavker, Y.V.2    Benedek, G.B.3
  • 19
    • 34548267115 scopus 로고    scopus 로고
    • Helix Self-Assembly from Anisotropic Molecules
    • Fejer, S. N.; Wales, D. J. Helix Self-Assembly from Anisotropic Molecules Phys. Rev. Lett. 2007, 99, 1-4
    • (2007) Phys. Rev. Lett. , vol.99 , pp. 1-4
    • Fejer, S.N.1    Wales, D.J.2
  • 23
    • 84875871051 scopus 로고    scopus 로고
    • Atomic Structure and Hierarchical Assembly of a Cross-θ Amyloid Fibril
    • Fitzpatrick, A. W. P. Atomic Structure and Hierarchical Assembly of a Cross-θ Amyloid Fibril Proc. Natl. Acad. Sci. U.S.A. 2013, 110, 5468-5473
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 5468-5473
    • Fitzpatrick, A.W.P.1
  • 24
    • 44349130859 scopus 로고    scopus 로고
    • Structural Transitions in Model Beta-Sheet Tapes
    • Bellesia, G.; Fedorov, M. V.; Timoshenko, E. G. Structural Transitions in Model Beta-Sheet Tapes J. Chem. Phys. 2008, 128, 195105
    • (2008) J. Chem. Phys. , vol.128 , pp. 195105
    • Bellesia, G.1    Fedorov, M.V.2    Timoshenko, E.G.3
  • 25
    • 0033200063 scopus 로고    scopus 로고
    • Protein Misfolding, Evolution and Disease
    • Dobson, C. M. Protein Misfolding, Evolution and Disease Trends Biochem. Sci. 1999, 24, 329-32
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 26
    • 0023430366 scopus 로고
    • Monte Carlo-Minimization Approach to the Multiple-Minima Problem in Protein Folding
    • Li, Z.; Scheraga, H. Monte Carlo-Minimization Approach to the Multiple-Minima Problem in Protein Folding Proc. Natl. Acad. Sci. U.S.A. 1987, 84, 6611-5
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6611-6615
    • Li, Z.1    Scheraga, H.2
  • 27
    • 0000560869 scopus 로고    scopus 로고
    • Global Optimization by Basin-Hopping and the Lowest Energy Structures of Lennard-Jones Clusters Containing up to 110 Atoms
    • Wales, D. J.; Doye, J. P. K. Global Optimization by Basin-Hopping and the Lowest Energy Structures of Lennard-Jones Clusters Containing up to 110 Atoms J. Phys. Chem. A 1997, 101, 5111-5116
    • (1997) J. Phys. Chem. A , vol.101 , pp. 5111-5116
    • Wales, D.J.1    Doye, J.P.K.2
  • 28
    • 0033610078 scopus 로고    scopus 로고
    • Global Optimization of Clusters, Crystals, and Biomolecules
    • Wales, D. J.; Scheraga, H. Global Optimization of Clusters, Crystals, and Biomolecules Science 1999, 285, 1368-1372
    • (1999) Science , vol.285 , pp. 1368-1372
    • Wales, D.J.1    Scheraga, H.2
  • 29
    • 85067718932 scopus 로고    scopus 로고
    • GMIN: A Program for Basin-Hopping Global Optimisation; (accessed November 2011)
    • Wales, D. J. GMIN: A Program for Basin-Hopping Global Optimisation; http://www-wales.ch.cam.ac.uk/software.html (accessed November 2011).
    • Wales, D.J.1
  • 30
    • 33846216327 scopus 로고    scopus 로고
    • The Directional Contact Distance of Two Ellipsoids: Coarse-Grained Potentials for Anisotropic Interactions
    • Paramonov, L.; Yaliraki, S. N. The Directional Contact Distance of Two Ellipsoids: Coarse-Grained Potentials for Anisotropic Interactions J. Chem. Phys. 2005, 123, 194111
    • (2005) J. Chem. Phys. , vol.123 , pp. 194111
    • Paramonov, L.1    Yaliraki, S.N.2
  • 31
    • 78049287226 scopus 로고    scopus 로고
    • Amyloid Structure-One but Not the Same: The Many Levels of Fibrillar Polymorphism
    • Pedersen, J. S.; Andersen, C. B.; Otzen, D. E. Amyloid Structure-One but Not the Same: the Many Levels of Fibrillar Polymorphism FEBS J. 2010, 277, 4591-601
    • (2010) FEBS J. , vol.277 , pp. 4591-4601
    • Pedersen, J.S.1    Andersen, C.B.2    Otzen, D.E.3
  • 32
    • 0024921948 scopus 로고
    • Defining the Axis of a Helix
    • Kahn, P. C. Defining the Axis of a Helix Comput. Chem. 1989, 13, 185-189
    • (1989) Comput. Chem. , vol.13 , pp. 185-189
    • Kahn, P.C.1
  • 33
    • 61549105950 scopus 로고    scopus 로고
    • Elastic Theory of Unconstrained Non-Euclidean Plates
    • Efrati, E.; Sharon, E.; Kupferman, R. Elastic Theory of Unconstrained Non-Euclidean Plates J. Mech. Phys. Sol. 2009, 57, 762-775
    • (2009) J. Mech. Phys. Sol. , vol.57 , pp. 762-775
    • Efrati, E.1    Sharon, E.2    Kupferman, R.3
  • 34
    • 77950288850 scopus 로고    scopus 로고
    • Relation between Serum Amyloid A Truncated Peptides and their Suprastructure Chirality
    • Rubin, N.; Perugia, E.; Wolf, S. G.; Klein, E.; Fridkin, M.; Addadi, L. Relation between Serum Amyloid A Truncated Peptides and their Suprastructure Chirality J. Am. Chem. Soc. 2010, 132, 4242-8
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4242-4248
    • Rubin, N.1    Perugia, E.2    Wolf, S.G.3    Klein, E.4    Fridkin, M.5    Addadi, L.6
  • 35
    • 51349113794 scopus 로고    scopus 로고
    • Revealing Molecular-Level Surface Structure of Amyloid Fibrils in Liquid by Means of Frequency Modulation Atomic Force Microscopy
    • Fukuma, T.; Mostaert, A. S.; Serpell, L. C.; Jarvis, S. P. Revealing Molecular-Level Surface Structure of Amyloid Fibrils in Liquid by Means of Frequency Modulation Atomic Force Microscopy Nanotechnology 2008, 19, 384010
    • (2008) Nanotechnology , vol.19 , pp. 384010
    • Fukuma, T.1    Mostaert, A.S.2    Serpell, L.C.3    Jarvis, S.P.4
  • 36
    • 57349120654 scopus 로고    scopus 로고
    • Structural Insights into the Polymorphism of Amyloid-Like Fibrils Formed by Region 20-29 of Amylin Revealed by Solid-State NMR and X-Ray Fiber Diffraction
    • Madine, J.; Jack, E.; Stockley, P. G.; Radford, S. E.; Serpell, L. C.; Middleton, D. a. Structural Insights into the Polymorphism of Amyloid-Like Fibrils Formed by Region 20-29 of Amylin Revealed by Solid-State NMR and X-Ray Fiber Diffraction J. Am. Chem. Soc. 2008, 130, 14990-5001
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14990-15001
    • Madine, J.1    Jack, E.2    Stockley, P.G.3    Radford, S.E.4    Serpell, L.C.5    Middleton, D.A.6
  • 37
    • 0017201915 scopus 로고
    • Tubulin-Nucleotide Interactions during the Polymerization and Depolymerization of Microtubules
    • Weisenberg, R. C.; Deery, W. J.; Dickinson, P. J. Tubulin-Nucleotide Interactions During the Polymerization and Depolymerization of Microtubules Biochemistry 1976, 15, 4248-54
    • (1976) Biochemistry , vol.15 , pp. 4248-4254
    • Weisenberg, R.C.1    Deery, W.J.2    Dickinson, P.J.3
  • 38
    • 84866266469 scopus 로고    scopus 로고
    • Heritable Yeast Prions Have a Highly Organized Three-Dimensional Architecture with Interfiber Structures
    • Saibil, H. R.; Seybert, A.; Habermann, A.; Winkler, J.; Eltsov, M.; Perkovic, M. Heritable Yeast Prions Have a Highly Organized Three-Dimensional Architecture with Interfiber Structures Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 14906-14911
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 14906-14911
    • Saibil, H.R.1    Seybert, A.2    Habermann, A.3    Winkler, J.4    Eltsov, M.5    Perkovic, M.6
  • 39
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for Electron TransferWithin and between Proteins
    • Page, C. C.; Moser, C. C.; Dutton, P. L. Mechanism for Electron TransferWithin and between Proteins Curr. Opin. Chem. Biol. 2003, 7, 551-556
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.