메뉴 건너뛰기




Volumn 26, Issue 9, 2014, Pages 580-587

Chirality and chiroptical properties of amyloid fibrils

Author keywords

beta sheet twist; fibril symmetry; filament; handedness; superstructural chirality; vibrational circular dichroism

Indexed keywords

AMINO ACID; AMYLOID; BOVINE SERUM ALBUMIN; POLYPEPTIDE;

EID: 84906820777     PISSN: 08990042     EISSN: 1520636X     Source Type: Journal    
DOI: 10.1002/chir.22335     Document Type: Conference Paper
Times cited : (34)

References (79)
  • 1
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fändrich M, Dobson CM,. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J 2002; 21: 5682-5690.
    • (2002) EMBO J , vol.21 , pp. 5682-5690
    • Fändrich, M.1    Dobson, C.M.2
  • 2
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky VN, Fink AL,. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim Biophys Acta 2004; 1698: 131-153.
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 3
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson CM,. Principles of protein folding, misfolding and aggregation. Semin Cell Dev Biol 2004; 15: 3-16.
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 4
    • 0028308104 scopus 로고
    • [URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • Wickner RB,. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 1994; 264: 566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • Wickner, R.B.1
  • 6
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin even an ordinary globular protein can assume a rogue guise if conditions are right
    • Fändrich M, Fletcher MA, Dobson CM,. Amyloid fibrils from muscle myoglobin Even an ordinary globular protein can assume a rogue guise if conditions are right. Nature 2001; 410: 165-166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 8
    • 0037044732 scopus 로고    scopus 로고
    • Charge attraction and β propensity are necessary for amyloid fibril formation from tetrapeptides
    • Tjernberg L, Hosia W, Bark N, Thyberg J, Johansson J,. Charge attraction and β propensity are necessary for amyloid fibril formation from tetrapeptides. J Biol Chem 2002; 277: 43243-43246.
    • (2002) J Biol Chem , vol.277 , pp. 43243-43246
    • Tjernberg, L.1    Hosia, W.2    Bark, N.3    Thyberg, J.4    Johansson, J.5
  • 9
    • 84890390405 scopus 로고    scopus 로고
    • Amyloid-like fibrils formed by ε-poly-l-lysine
    • Lai J, Zheng C, Liang D, Huang Y,. Amyloid-like fibrils formed by ε-poly-l-lysine. Biomacromolecules 2013; 14: 4515-4519.
    • (2013) Biomacromolecules , vol.14 , pp. 4515-4519
    • Lai, J.1    Zheng, C.2    Liang, D.3    Huang, Y.4
  • 10
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe JD, Cohen AS,. Review: History of the amyloid fibril. J Struct Biol 2000; 130: 88-98.
    • (2000) J Struct Biol , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 14
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • Serpell LC,. Alzheimer's amyloid fibrils: Structure and assembly. BBA-Mol Basis Dis 2000; 1502: 16-30.
    • (2000) BBA-Mol Basis Dis , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 15
    • 0015914783 scopus 로고
    • Conformation of twisted β-pleated sheets in proteins
    • Chothia C., Conformation of twisted β-pleated sheets in proteins. J Mol Biol 1973; 75: 295-302.
    • (1973) J Mol Biol , vol.75 , pp. 295-302
    • Chothia, C.1
  • 16
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson JS,. The anatomy and taxonomy of protein structure. Adv Protein Chem 1981; 34: 167-339.
    • (1981) Adv Protein Chem , vol.34 , pp. 167-339
    • Richardson, J.S.1
  • 17
    • 77950288850 scopus 로고    scopus 로고
    • Relation between serum amyloid A truncated peptides and their suprastructure chirality
    • Rubin N, Perugia E, Wolf SG, Klein E, Fridkin M, Addadi L,. Relation between serum amyloid A truncated peptides and their suprastructure chirality. J Am Chem Soc 2010; 132: 4242-4248.
    • (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
  • 20
    • 1642299396 scopus 로고    scopus 로고
    • The diastereomeric assembly of polylysine is the low-volume pathway for preferential formation of β-sheet aggregates
    • Dzwolak W, Ravindra R, Nicolini C, Jansen R, Winter R,. The diastereomeric assembly of polylysine is the low-volume pathway for preferential formation of β-sheet aggregates. J Am Chem Soc 2004; 126: 3762-3768.
    • (2004) J Am Chem Soc , vol.126 , pp. 3762-3768
    • Dzwolak, W.1    Ravindra, R.2    Nicolini, C.3    Jansen, R.4    Winter, R.5
  • 21
    • 17444390052 scopus 로고    scopus 로고
    • A conformational alpha-helix to beta-sheet transition accompanies racemic self-assembly of polylysine: An FT-IR spectroscopic study
    • Dzwolak W, Smirnovas V,. A conformational alpha-helix to beta-sheet transition accompanies racemic self-assembly of polylysine: an FT-IR spectroscopic study. Biophys Chem 2005; 115: 49-54.
    • (2005) Biophys Chem , vol.115 , pp. 49-54
    • Dzwolak, W.1    Smirnovas, V.2
  • 22
    • 84860498820 scopus 로고    scopus 로고
    • An FT-IR study on packing defects in mixed β-aggregates of poly(L-glutamic acid) and poly(D-glutamic acid): A high-pressure rescue from a kinetic trap
    • Yamaoki Y, Imamura H, Fulara A, Wojcik S, BozyckiL, Kato M, Keiderling TA, Dzwolak W,. An FT-IR study on packing defects in mixed β-aggregates of poly(L-glutamic acid) and poly(D-glutamic acid): A high-pressure rescue from a kinetic trap. J Phys Chem B 2012; 116: 5172-5178.
    • (2012) J Phys Chem B , vol.116 , pp. 5172-5178
    • Yamaoki, Y.1    Imamura, H.2    Fulara, A.3    Wojcik, S.4    Bozyckil, K.M.5    Keiderling, T.A.6    Dzwolak, W.7
  • 23
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
    • Harper JD, Lieber CM, Lansbury PT,. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein. Chem Biol 1997; 4: 951-959.
    • (1997) Chem Biol , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 26
    • 0028800177 scopus 로고
    • Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin
    • Bauer HH, Aebi U, Häner M, Hermann R, Müller M, Arvinte T, Merkle HP,. Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. J Struct Biol 1995; 115: 1-15.
    • (1995) J Struct Biol , vol.115 , pp. 1-15
    • Bauer, H.H.1    Aebi, U.2    Häner, M.3    Hermann, R.4    Müller, M.5    Arvinte, T.6    Merkle, H.P.7
  • 30
    • 84880550029 scopus 로고    scopus 로고
    • A left-handed building block self-assembles into right- and left-handed helices
    • Olesen SW, Fejer SN, Chakrabarti D, Wales DJ,. A left-handed building block self-assembles into right- and left-handed helices. RSC Adv 2013; 3: 12905-12908.
    • (2013) RSC Adv , vol.3 , pp. 12905-12908
    • Olesen, S.W.1    Fejer, S.N.2    Chakrabarti, D.3    Wales, D.J.4
  • 31
    • 84881156013 scopus 로고    scopus 로고
    • Chirality inversions in self-assembly of fibrillar superstructures: A computational study
    • Gruziel M, Dzwolak W, Szymczak P,. Chirality inversions in self-assembly of fibrillar superstructures: A computational study. Soft Matter 2013; 9: 8005-8013.
    • (2013) Soft Matter , vol.9 , pp. 8005-8013
    • Gruziel, M.1    Dzwolak, W.2    Szymczak, P.3
  • 32
    • 84881477404 scopus 로고    scopus 로고
    • Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates
    • Ghattyvenkatakrishna PK, Uberbacher EC, Cheng X,. Effect of the amyloid β hairpin's structure on the handedness of helices formed by its aggregates. FEBS Lett 2013; 587: 2649-2655.
    • (2013) FEBS Lett , vol.587 , pp. 2649-2655
    • Ghattyvenkatakrishna, P.K.1    Uberbacher, E.C.2    Cheng, X.3
  • 33
    • 33846160381 scopus 로고    scopus 로고
    • Polymorphism in the intermediates and products of amyloid assembly
    • Kodali R, Wetzel R,. Polymorphism in the intermediates and products of amyloid assembly. Curr Opin Struct Biol 2007; 17: 48-57.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 48-57
    • Kodali, R.1    Wetzel, R.2
  • 34
    • 84891368203 scopus 로고    scopus 로고
    • A clear view of polymorphism, twist, and chirality in amyloid fibril formation
    • Volpatti LR, Vendruscolo M, Dobson CM, Knowles TPJ,. A clear view of polymorphism, twist, and chirality in amyloid fibril formation. ACS Nano 2013; 7: 10443-10448.
    • (2013) ACS Nano , vol.7 , pp. 10443-10448
    • Volpatti, L.R.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.J.4
  • 35
    • 79957477372 scopus 로고    scopus 로고
    • Adjustable twisting periodic pitch of amyloid fibrils
    • Adamcik J, Mezzenga R,. Adjustable twisting periodic pitch of amyloid fibrils. Soft Matter 2011; 7: 5437-5443.
    • (2011) Soft Matter , vol.7 , pp. 5437-5443
    • Adamcik, J.1    Mezzenga, R.2
  • 36
    • 77955230701 scopus 로고    scopus 로고
    • Understanding amyloid aggregation by statistical analysis of atomic force microscopy images
    • Adamcik J, Jung JM, Flakowski J, De Los Rios P, Dietler G, Mezzenga R,. Understanding amyloid aggregation by statistical analysis of atomic force microscopy images. Nat Nanotechnol 2010; 5: 423-428.
    • (2010) Nat Nanotechnol , vol.5 , pp. 423-428
    • Adamcik, J.1    Jung, J.M.2    Flakowski, J.3    De Los, R.P.4    Dietler, G.5    Mezzenga, R.6
  • 37
    • 79955863547 scopus 로고    scopus 로고
    • General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons
    • Lara C, Adamcik J, Jordens S, Mezzenga R,. General self-assembly mechanism converting hydrolyzed globular proteins into giant multistranded amyloid ribbons. Biomacromolecules 2011; 12: 1868-1875.
    • (2011) Biomacromolecules , vol.12 , pp. 1868-1875
    • Lara, C.1    Adamcik, J.2    Jordens, S.3    Mezzenga, R.4
  • 38
    • 84880899843 scopus 로고    scopus 로고
    • Towards lysozyme nanotube and 3D hybrid self-assembly
    • Lara C, Handschin S, Mezzenga R,. Towards lysozyme nanotube and 3D hybrid self-assembly. Nanoscale 2013; 5: 7197-7201.
    • (2013) Nanoscale , vol.5 , pp. 7197-7201
    • Lara, C.1    Handschin, S.2    Mezzenga, R.3
  • 39
    • 84891362825 scopus 로고    scopus 로고
    • Polymorphism complexity and handedness inversion in serum albumin amyloid fibrils
    • Usov I, Adamcik J, Mezzenga R,. Polymorphism complexity and handedness inversion in serum albumin amyloid fibrils. ACS Nano 2013; 7: 10465-10474.
    • (2013) ACS Nano , vol.7 , pp. 10465-10474
    • Usov, I.1    Adamcik, J.2    Mezzenga, R.3
  • 40
    • 0034636977 scopus 로고    scopus 로고
    • Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme
    • Blanch EW, Morozova-Roche LA, Cochran DAE, Doig AJ, Hecht L, Barron LD,. Is polyproline II helix the killer conformation? A Raman optical activity study of the amyloidogenic prefibrillar intermediate of human lysozyme. J Mol Biol 2000; 301: 553-563.
    • (2000) J Mol Biol , vol.301 , pp. 553-563
    • Blanch, E.W.1    Morozova-Roche, L.A.2    Cochran, D.A.E.3    Doig, A.J.4    Hecht, L.5    Barron, L.D.6
  • 41
    • 4644372554 scopus 로고    scopus 로고
    • Raman optical activity demonstrates poly(l-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction
    • Blanch EW, Gill AC, Rhie AGO, Hope J, Hecht L, Nielsen K, Barron LD,. Raman optical activity demonstrates poly(l-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction. J Mol Biol 2004; 343: 467-476.
    • (2004) J Mol Biol , vol.343 , pp. 467-476
    • Blanch, E.W.1    Gill, A.C.2    Rhie, A.G.O.3    Hope, J.4    Hecht, L.5    Nielsen, K.6    Barron, L.D.7
  • 42
    • 84855516998 scopus 로고    scopus 로고
    • Raman optical activity study on insulin amyloid- and prefibril intermediate
    • Yamamoto S, Watarai H,. Raman optical activity study on insulin amyloid- and prefibril intermediate. Chirality 2012; 24: 97-103.
    • (2012) Chirality , vol.24 , pp. 97-103
    • Yamamoto, S.1    Watarai, H.2
  • 43
    • 0035471627 scopus 로고    scopus 로고
    • A solid-state dedicated circular dichroism spectrophotometer: Development and application
    • Kuroda R, Harada T, Shindo Y,. A solid-state dedicated circular dichroism spectrophotometer: Development and application. Rev Sci Instrum 2001; 72: 3802-3810.
    • (2001) Rev Sci Instrum , vol.72 , pp. 3802-3810
    • Kuroda, R.1    Harada, T.2    Shindo, Y.3
  • 45
    • 0020770309 scopus 로고
    • Circular differential scattering can be an important part of the circular dichroism of macromolecules
    • Bustamante C, Tinoco I, Maestre MF,. Circular differential scattering can be an important part of the circular dichroism of macromolecules. Proc Natl Acad Sci U S A 1983; 80: 3568-3572.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 3568-3572
    • Bustamante, C.1    Tinoco, I.2    Maestre, M.F.3
  • 46
    • 78649652839 scopus 로고    scopus 로고
    • CD measurements of β-amyloid (1-40) and (1-42) in the condensed phase
    • Harada T, Kuroda R,. CD measurements of β-amyloid (1-40) and (1-42) in the condensed phase. Biopolymers 2011; 95: 127-134.
    • (2011) Biopolymers , vol.95 , pp. 127-134
    • Harada, T.1    Kuroda, R.2
  • 49
    • 0024065282 scopus 로고
    • Circular dichroism studies of distorted α-helices, twisted β-sheets, and β-turns
    • Manning MC, Illangasekare M, Woody RW,. Circular dichroism studies of distorted α-helices, twisted β-sheets, and β-turns. Biophys Chem 1988; 31: 77-86.
    • (1988) Biophys Chem , vol.31 , pp. 77-86
    • Manning, M.C.1    Illangasekare, M.2    Woody, R.W.3
  • 50
    • 75649120781 scopus 로고    scopus 로고
    • Influence of the solvent on the self-assembly of a modified amyloid beta peptide fragment. II. NMR and computer simulation investigation
    • Hamley IW, Nutt DR, Brown GD, Miravet JF, Escuder B, Rodríguez- Llansola F,. Influence of the solvent on the self-assembly of a modified amyloid beta peptide fragment. II. NMR and computer simulation investigation. J Phys Chem B 2010; 114: 940-951.
    • (2010) J Phys Chem B , vol.114 , pp. 940-951
    • Hamley, I.W.1    Nutt, D.R.2    Brown, G.D.3    Miravet, J.F.4    Escuder, B.5    Rodríguez-Llansola, F.6
  • 51
    • 84876759904 scopus 로고    scopus 로고
    • Tuning nanostructure dimensions with supramolecular twisting
    • Moyer TJ, Cui H, Stupp SI,. Tuning nanostructure dimensions with supramolecular twisting. J Phys Chem B 2013; 117: 4604-4610.
    • (2013) J Phys Chem B , vol.117 , pp. 4604-4610
    • Moyer, T.J.1    Cui, H.2    Stupp, S.I.3
  • 52
    • 0014836203 scopus 로고
    • Congo red dichroism with dispersed amyloid fibrils, an extrinsic Cotton effect
    • Benditt EP, Eriksen N, Berglund C,. Congo red dichroism with dispersed amyloid fibrils, an extrinsic Cotton effect. Proc Natl Acad Sci U S A 1970; 66: 1044-1051.
    • (1970) Proc Natl Acad Sci U S A , vol.66 , pp. 1044-1051
    • Benditt, E.P.1    Eriksen, N.2    Berglund, C.3
  • 55
    • 27944455577 scopus 로고    scopus 로고
    • Chiral bias of amyloid fibrils revealed by the twisted conformation of thioflavin T: An induced circular dichroism / DFT study
    • Dzwolak W, Pecul M,. Chiral bias of amyloid fibrils revealed by the twisted conformation of thioflavin T: an induced circular dichroism / DFT study. FEBS Lett 2005; 579: 6601-6603.
    • (2005) FEBS Lett , vol.579 , pp. 6601-6603
    • Dzwolak, W.1    Pecul, M.2
  • 56
    • 34250897912 scopus 로고    scopus 로고
    • Conformational indeterminism in protein misfolding: Chiral amplification on amyloidogenic pathway of insulin
    • Dzwolak W, Loksztejn A, Galinska-Rakoczy A, Adachi R, Goto Y, Rupnicki L,. Conformational indeterminism in protein misfolding: chiral amplification on amyloidogenic pathway of insulin. J Am Chem Soc 2007; 129: 7517-7522.
    • (2007) J Am Chem Soc , vol.129 , pp. 7517-7522
    • Dzwolak, W.1    Loksztejn, A.2    Galinska-Rakoczy, A.3    Adachi, R.4    Goto, Y.5    Rupnicki, L.6
  • 57
    • 42749089759 scopus 로고    scopus 로고
    • Chiral bifurcation in aggregating insulin: An induced circular dichroism study
    • Loksztejn A, Dzwolak W,. Chiral bifurcation in aggregating insulin: An induced circular dichroism study. J Mol Biol 2008; 379: 9-16.
    • (2008) J Mol Biol , vol.379 , pp. 9-16
    • Loksztejn, A.1    Dzwolak, W.2
  • 58
    • 73249149528 scopus 로고    scopus 로고
    • Vortex-induced formation of insulin amyloid superstructures probed by time-lapse atomic force microscopy and circular dichroism spectroscopy
    • Loksztejn A, Dzwolak W,. Vortex-induced formation of insulin amyloid superstructures probed by time-lapse atomic force microscopy and circular dichroism spectroscopy. J Mol Biol 2010; 395: 643-655.
    • (2010) J Mol Biol , vol.395 , pp. 643-655
    • Loksztejn, A.1    Dzwolak, W.2
  • 59
    • 0000881952 scopus 로고
    • Chiral symmetry breaking in sodium chlorate crystallization
    • Kondepudi DK, Kaufman RJ, Singh N,. Chiral symmetry breaking in sodium chlorate crystallization. Science 1990; 250: 975-976.
    • (1990) Science , vol.250 , pp. 975-976
    • Kondepudi, D.K.1    Kaufman, R.J.2    Singh, N.3
  • 60
    • 18144376283 scopus 로고    scopus 로고
    • Chiral symmetry breaking during crystallization: Complete chiral purity induced by nonlinear autocatalysis and recycling
    • art.no. 065504.
    • Viedma C., Chiral symmetry breaking during crystallization: Complete chiral purity induced by nonlinear autocatalysis and recycling. Phys Rev Lett 2005; 94:art.no. 065504.
    • (2005) Phys Rev Lett , vol.94
    • Viedma, C.1
  • 61
    • 84875225883 scopus 로고    scopus 로고
    • Amino acid sequence determinants in self-assembly of insulin chiral amyloid superstructures: Role of C-terminus of B-chain in association of fibrils
    • Babenko V, Dzwolak W,. Amino acid sequence determinants in self-assembly of insulin chiral amyloid superstructures: Role of C-terminus of B-chain in association of fibrils. FEBS Lett 2013; 587: 625-630.
    • (2013) FEBS Lett , vol.587 , pp. 625-630
    • Babenko, V.1    Dzwolak, W.2
  • 62
    • 84877043688 scopus 로고    scopus 로고
    • Vortex-induced amyloid superstructures of insulin and its component A and B chains
    • Babenko V, Piejko M, Wõjcik S, Mak P, Dzwolak W,. Vortex-induced amyloid superstructures of insulin and its component A and B chains. Langmuir 2013; 29: 5271-5278.
    • (2013) Langmuir , vol.29 , pp. 5271-5278
    • Babenko, V.1    Piejko, M.2    Wõjcik, S.3    Mak, P.4    Dzwolak, W.5
  • 64
    • 35349023009 scopus 로고    scopus 로고
    • Vibrational circular dichroism shows unusual sensitivity to protein fibril formation and development in solution
    • Ma S, Cao X, Mak M, Sadik A, Walkner C, Freedman TB, Lednev IK, Dukor RK, Nafie LA,. Vibrational circular dichroism shows unusual sensitivity to protein fibril formation and development in solution. J Am Chem Soc 2007; 129: 12364-12365.
    • (2007) J Am Chem Soc , vol.129 , pp. 12364-12365
    • Ma, S.1    Cao, X.2    Mak, M.3    Sadik, A.4    Walkner, C.5    Freedman, T.B.6    Lednev, I.K.7    Dukor, R.K.8    Nafie, L.A.9
  • 65
    • 77956812220 scopus 로고    scopus 로고
    • Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism
    • Kurouski D, Lombardi RA, Dukor RK, Lednev IK, Nafie LA,. Direct observation and pH control of reversed supramolecular chirality in insulin fibrils by vibrational circular dichroism. Chem Commun 2010; 46: 7154-7156.
    • (2010) Chem Commun , vol.46 , pp. 7154-7156
    • Kurouski, D.1    Lombardi, R.A.2    Dukor, R.K.3    Lednev, I.K.4    Nafie, L.A.5
  • 67
    • 84864686797 scopus 로고    scopus 로고
    • Normal and reversed supramolecular chirality of insulin fibrils probed by vibrational circular dichroism at the protofilament level of fibril structure
    • Kurouski D, Dukor RK, Lu X, Nafie LA, Lednev IK,. Normal and reversed supramolecular chirality of insulin fibrils probed by vibrational circular dichroism at the protofilament level of fibril structure. Biophys J 2012; 103: 522-531.
    • (2012) Biophys J , vol.103 , pp. 522-531
    • Kurouski, D.1    Dukor, R.K.2    Lu, X.3    Nafie, L.A.4    Lednev, I.K.5
  • 69
    • 80053383864 scopus 로고    scopus 로고
    • Isotope-assisted vibrational circular dichroism investigations of amyloid β peptide fragment, Aβ(16-22)
    • Shanmugam G, Polavarapu PL,. Isotope-assisted vibrational circular dichroism investigations of amyloid β peptide fragment, Aβ(16-22). J Struct Biol 2011; 176: 212-219.
    • (2011) J Struct Biol , vol.176 , pp. 212-219
    • Shanmugam, G.1    Polavarapu, P.L.2
  • 71
    • 84878242530 scopus 로고    scopus 로고
    • Levels of supramolecular chirality of polyglutamine aggregates revealed by vibrational circular dichroism
    • Kurouski D, Kar K, Wetzel R, Dukor RK, Lednev IK, Nafie LA,. Levels of supramolecular chirality of polyglutamine aggregates revealed by vibrational circular dichroism. FEBS Lett 2013; 587: 1638-1643.
    • (2013) FEBS Lett , vol.587 , pp. 1638-1643
    • Kurouski, D.1    Kar, K.2    Wetzel, R.3    Dukor, R.K.4    Lednev, I.K.5    Nafie, L.A.6
  • 72
    • 80052823373 scopus 로고    scopus 로고
    • Spiral superstructures of amyloid-like fibrils of polyglutamic acid: An infrared absorption and vibrational circular dichroism study
    • Fulara A, Lakhani A, Wõjcik S, Nieznaska H, Keiderling TA, Dzwolak W,. Spiral superstructures of amyloid-like fibrils of polyglutamic acid: An infrared absorption and vibrational circular dichroism study. J Phys Chem B 2011; 115: 11010-11016.
    • (2011) J Phys Chem B , vol.115 , pp. 11010-11016
    • Fulara, A.1    Lakhani, A.2    Wõjcik, S.3    Nieznaska, H.4    Keiderling, T.A.5    Dzwolak, W.6
  • 73
    • 84887576417 scopus 로고    scopus 로고
    • Insight into the packing pattern of β2 fibrils: A model study of glutamic acid rich oligomers with 13C isotopic edited vibrational spectroscopy
    • Chi H, Welch WRW, Kubelka J, Keiderling TA,. Insight into the packing pattern of β2 fibrils: A model study of glutamic acid rich oligomers with 13C isotopic edited vibrational spectroscopy. Biomacromolecules 2013; 14: 3880-3891.
    • (2013) Biomacromolecules , vol.14 , pp. 3880-3891
    • Chi, H.1    Welch, W.R.W.2    Kubelka, J.3    Keiderling, T.A.4
  • 74
    • 73249133310 scopus 로고    scopus 로고
    • Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal
    • Measey TJ, Smith KB, Decatur SM, Zhao L, Yang G, Schweitzer-Stenner R,. Self-aggregation of a polyalanine octamer promoted by its C-terminal tyrosine and probed by a strongly enhanced vibrational circular dichroism signal. J Am Chem Soc 2009; 131: 18218-18219.
    • (2009) J Am Chem Soc , vol.131 , pp. 18218-18219
    • Measey, T.J.1    Smith, K.B.2    Decatur, S.M.3    Zhao, L.4    Yang, G.5    Schweitzer-Stenner, R.6
  • 75
    • 79851507329 scopus 로고    scopus 로고
    • Vibrational circular dichroism as a probe of fibrillogenesis: The origin of the anomalous intensity enhancement of amyloid-like fibrils
    • Measey TJ, Schweitzer-Stenner R,. Vibrational circular dichroism as a probe of fibrillogenesis: The origin of the anomalous intensity enhancement of amyloid-like fibrils. J Am Chem Soc 2011; 133: 1066-1076.
    • (2011) J Am Chem Soc , vol.133 , pp. 1066-1076
    • Measey, T.J.1    Schweitzer-Stenner, R.2
  • 76
    • 84884171827 scopus 로고    scopus 로고
    • Infrared, vibrational circular dichroism, and Raman spectral simulations for β-sheet structures with various isotopic labels, interstrand, and stacking arrangements using density functional theory
    • Welch WRW, Kubelka J, Keiderling TA,. Infrared, vibrational circular dichroism, and Raman spectral simulations for β-sheet structures with various isotopic labels, interstrand, and stacking arrangements using density functional theory. J Phys Chem B 2013; 117: 10343-10358.
    • (2013) J Phys Chem B , vol.117 , pp. 10343-10358
    • Welch, W.R.W.1    Kubelka, J.2    Keiderling, T.A.3
  • 77
    • 84884190571 scopus 로고    scopus 로고
    • Structural analyses of experimental 13C edited amide I' IR and VCD for peptide β-sheet aggregates and fibrils using DFT-based spectral simulations
    • Welch WRW, Keiderling TA, Kubelka J,. Structural analyses of experimental 13C edited amide I' IR and VCD for peptide β-sheet aggregates and fibrils using DFT-based spectral simulations. J Phys Chem B 2013; 117: 10359-10369.
    • (2013) J Phys Chem B , vol.117 , pp. 10359-10369
    • Welch, W.R.W.1    Keiderling, T.A.2    Kubelka, J.3
  • 79
    • 84862841611 scopus 로고    scopus 로고
    • Protein nanofibrils balance colours in organic white-light-emitting diodes
    • Solin N, Inganäs O,. Protein nanofibrils balance colours in organic white-light-emitting diodes. Isr J Chem 2012; 52: 529-539.
    • (2012) Isr J Chem , vol.52 , pp. 529-539
    • Solin, N.1    Inganäs, O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.