메뉴 건너뛰기




Volumn 1753, Issue 1, 2005, Pages 100-107

FT-IR approaches on amyloid fibril structure

Author keywords

Amide I; Amyloid fibril structure; FT IR; IR linear dichroism; Isotope label; Microscope

Indexed keywords

AMIDE; AMYLOID; ISOTOPE; PEPTIDE;

EID: 27744577906     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.07.008     Document Type: Conference Paper
Times cited : (116)

References (72)
  • 1
    • 0026642332 scopus 로고
    • Aggregation of chymotrypsinogen-portrait by infrared-spectroscopy
    • A.A. Ismail, H.H. Mantsch, and P.T.T. Wong Aggregation of chymotrypsinogen-portrait by infrared-spectroscopy Biochim. Biophys. Acta 1121 1992 183 188
    • (1992) Biochim. Biophys. Acta , vol.1121 , pp. 183-188
    • Ismail, A.A.1    Mantsch, H.H.2    Wong, P.T.T.3
  • 2
    • 0000005909 scopus 로고
    • Time-resolved step-scan FT-IR investigations of the transition from KL to L in the bacteriorhodopsin photocycle-Identification of chromophore twists by assigning hydrogen-out-of-plane (HOOP) bending vibrations
    • O. Weidlich, and F. Siebert Time-resolved step-scan FT-IR investigations of the transition from KL to L in the bacteriorhodopsin photocycle- Identification of chromophore twists by assigning hydrogen-out-of-plane (HOOP) bending vibrations Appl. Spectrosc. 47 1993 1394 1400
    • (1993) Appl. Spectrosc. , vol.47 , pp. 1394-1400
    • Weidlich, O.1    Siebert, F.2
  • 3
    • 0001300576 scopus 로고
    • Vibrational stark effect spectroscopy
    • A. Chattopadhyay, and S.G. Boxer Vibrational stark effect spectroscopy J. Am. Chem. Soc. 117 1995 1449 1450
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 1449-1450
    • Chattopadhyay, A.1    Boxer, S.G.2
  • 4
    • 2342643475 scopus 로고    scopus 로고
    • Development of infrared electroabsorption spectroscopy and its application to molecular structural studies
    • H. Hiramatsu, and H. Hamaguchi Development of infrared electroabsorption spectroscopy and its application to molecular structural studies Appl. Spectrosc. 58 2004 366
    • (2004) Appl. Spectrosc. , vol.58 , pp. 366
    • Hiramatsu, H.1    Hamaguchi, H.2
  • 6
    • 0035955555 scopus 로고    scopus 로고
    • 2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro
    • 2-microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro J. Mol. Biol. 313 2001 559 571
    • (2001) J. Mol. Biol. , vol.313 , pp. 559-571
    • Kad, N.M.1    Thomson, N.H.2    Smith, D.P.3    Smith, D.A.4    Radford, S.E.5
  • 7
    • 0042847751 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
    • J.L. Jimenez, J.I. Guijarro, E. Orlova, J. Zurdo, C.M. Dobson, M. Sunde, and H.R. Saibil Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing EMBO J. 18 1999 815 821
    • (1999) EMBO J. , vol.18 , pp. 815-821
    • Jimenez, J.L.1    Guijarro, J.I.2    Orlova, E.3    Zurdo, J.4    Dobson, C.M.5    Sunde, M.6    Saibil, H.R.7
  • 9
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • C. Blake, and L. Serpell Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix Structure 4 1996 989 998
    • (1996) Structure , vol.4 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 12
    • 4243898367 scopus 로고
    • Perturbation treatment of the characteristic vibrations of polypeptide chains in various configurations
    • T. Miyazawa Perturbation treatment of the characteristic vibrations of polypeptide chains in various configurations J. Chem. Phys. 32 1960 1647 1652
    • (1960) J. Chem. Phys. , vol.32 , pp. 1647-1652
    • Miyazawa, T.1
  • 13
    • 0343532738 scopus 로고
    • The infrared spectra of polypeptides in various conformations: Amide I and II bands
    • T. Miyazawa, and E.R. Blout The infrared spectra of polypeptides in various conformations: amide I and II bands J. Am. Chem. Soc. 83 1961 712 719
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 712-719
    • Miyazawa, T.1    Blout, E.R.2
  • 14
    • 0016721511 scopus 로고
    • Transition dipole coupling in amide I modes of β polypeptides
    • W.H. Moore, and S. Krimm Transition dipole coupling in amide I modes of β polypeptides Proc. Natl. Acad. Sci. U. S. A. 72 1975 4933 4935
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , pp. 4933-4935
    • Moore, W.H.1    Krimm, S.2
  • 15
    • 0017288712 scopus 로고
    • Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain preated sheet
    • Y.N. Chirgadze, and N.A. Nevskaya Infrared spectra and resonance interaction of amide-I vibration of the antiparallel-chain preated sheet Biopolymers 15 1976 607 625
    • (1976) Biopolymers , vol.15 , pp. 607-625
    • Chirgadze, Y.N.1    Nevskaya, N.A.2
  • 16
    • 11844282802 scopus 로고    scopus 로고
    • A quantitative reconstruction of the amide I contour in the IR spectra of globular proteins: From structure to spectrum
    • J.W. Brauner, C.R. Flach, and R. Mendelsohn A quantitative reconstruction of the amide I contour in the IR spectra of globular proteins: from structure to spectrum J. Am. Chem. Soc. 127 2005 100 109
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 100-109
    • Brauner, J.W.1    Flach, C.R.2    Mendelsohn, R.3
  • 17
    • 36449001245 scopus 로고
    • Model calculations on the amide-I infrared bands of globular proteins
    • H. Torii, and M. Tasumi Model calculations on the amide-I infrared bands of globular proteins J. Chem. Phys. 96 1992 3379 3387
    • (1992) J. Chem. Phys. , vol.96 , pp. 3379-3387
    • Torii, H.1    Tasumi, M.2
  • 18
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • D.M. Byler, and H. Susi Examination of the secondary structure of proteins by deconvolved FTIR spectra Biopolymers 25 1986 469 487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 19
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • A. Dong, P. Huang, and W.S. Caughey Protein secondary structures in water from second-derivative amide I infrared spectra Biochemistry 29 1990 3303 3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 20
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • J. Bandekar Amide modes and protein conformation Biochim. Biophys. Acta 1120 1992 123 143
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 123-143
    • Bandekar, J.1
  • 21
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using Fourier transform IR spectroscopy
    • P.I. Haris, and D. Chapman The conformational analysis of peptides using Fourier transform IR spectroscopy Biopolymers 37 1995 251 263
    • (1995) Biopolymers , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 22
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • S. Krimm, and J. Bandekar Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins Adv. Protein Chem. 38 1986 181 364
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 23
    • 0028909764 scopus 로고
    • Infrared spectroscopy applied to biochemical and biological problems
    • F. Siebert Infrared spectroscopy applied to biochemical and biological problems Methods Enzymol. 246 1995 501 526
    • (1995) Methods Enzymol. , vol.246 , pp. 501-526
    • Siebert, F.1
  • 24
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • B.W. Caughey, A. Dong, K.S. Bhat, D. Ernst, S.F. Hayes, and W.S. Caughey Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy Biochemistry 30 1991 7672 7680
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 25
    • 0024595103 scopus 로고
    • Comparison of the secondary structures of human class I and class II major histocompatibility complex antigens by Fourier transform infrared and circular dichroism spectroscopy
    • J.C. Gorga, A. Dong, M.C. Manning, R.W. Woody, W.S. Caughey, and J.L. Strominger Comparison of the secondary structures of human class I and class II major histocompatibility complex antigens by Fourier transform infrared and circular dichroism spectroscopy Proc. Natl. Acad. Sci. U. S. A. 86 1989 2321 2325
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 2321-2325
    • Gorga, J.C.1    Dong, A.2    Manning, M.C.3    Woody, R.W.4    Caughey, W.S.5    Strominger, J.L.6
  • 26
    • 0024997389 scopus 로고
    • Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods
    • F. Dousseau, and M. Pezolet Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods Biochemistry 29 1990 8771 8779
    • (1990) Biochemistry , vol.29 , pp. 8771-8779
    • Dousseau, F.1    Pezolet, M.2
  • 27
    • 1542357647 scopus 로고    scopus 로고
    • A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods
    • S.W. Cai, and B.R. Singh A distinct utility of the amide III infrared band for secondary structure estimation of aqueous protein solutions using partial least squares methods Biochemistry 43 2004 2541 2549
    • (2004) Biochemistry , vol.43 , pp. 2541-2549
    • Cai, S.W.1    Singh, B.R.2
  • 28
    • 0028539766 scopus 로고
    • Secondary structure estimation of proteins using the Amide III region of Fourier-transform infrared-spectroscopy-application to analyze calcium binding-induced structural-changes in calsequestrin
    • F.N. Fu, D.B. Deoliveira, W.A. Trumble, H.K. Sarkar, and B.R. Singh Secondary structure estimation of proteins using the Amide III region of Fourier-transform infrared-spectroscopy-application to analyze calcium binding-induced structural-changes in calsequestrin Appl. Spectrosc. 48 1994 1432 1441
    • (1994) Appl. Spectrosc. , vol.48 , pp. 1432-1441
    • Fu, F.N.1    Deoliveira, D.B.2    Trumble, W.A.3    Sarkar, H.K.4    Singh, B.R.5
  • 29
    • 0025613794 scopus 로고
    • 2O) solutions: I. Spectral parameters of amino acid residue absorption bands
    • 2O) solutions: I. Spectral parameters of amino acid residue absorption bands Biopolymers 30 1990 1243 1257
    • (1990) Biopolymers , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 30
    • 0027492164 scopus 로고
    • Determination of protein secondary structure by Fourier transform infrared spectroscopy: A critical assessment
    • W.K. Surewicz, H.H. Mantsch, and D. Chapman Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment Biochemistry 32 1993 389 394
    • (1993) Biochemistry , vol.32 , pp. 389-394
    • Surewicz, W.K.1    Mantsch, H.H.2    Chapman, D.3
  • 31
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra
    • W.K. Surewicz, and H.H. Mantsch New insight into protein secondary structure from resolution-enhanced infrared spectra Biochim. Biophys. Acta 952 1988 115 130
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 32
    • 0024467352 scopus 로고
    • Conformational transitions in poly(l-lysine): Studies using Fourier transform infrared spectroscopy
    • M. Jackson, P.I. Haris, and D. Chapman Conformational transitions in poly(l-lysine): studies using Fourier transform infrared spectroscopy Biochim. Biophys. Acta 998 1989 75 79
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 75-79
    • Jackson, M.1    Haris, P.I.2    Chapman, D.3
  • 33
    • 0031070340 scopus 로고    scopus 로고
    • Infrared spectroscopy in aqueous solution: Difficulties and accuracy of water subtraction
    • K. Rahmelow, and W. Huebner Infrared spectroscopy in aqueous solution: difficulties and accuracy of water subtraction Appl. Spectrosc. 51 1997 160 170
    • (1997) Appl. Spectrosc. , vol.51 , pp. 160-170
    • Rahmelow, K.1    Huebner, W.2
  • 34
    • 0033596301 scopus 로고    scopus 로고
    • Isotope-edited infrared spectroscopy of helical peptides
    • S.M. Decatur, and J. Antonic Isotope-edited infrared spectroscopy of helical peptides J. Am. Chem. Soc. 121 1999 11914 11915
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11914-11915
    • Decatur, S.M.1    Antonic, J.2
  • 35
    • 0037168451 scopus 로고    scopus 로고
    • The organization and assembly of a β-sheet formed by a prion peptide in solution: An isotope-edited FTIR study
    • R.A.G.D. Silva, J.Y. Nguyen, and S.M. Decatur The organization and assembly of a β-sheet formed by a prion peptide in solution: an isotope-edited FTIR study Biochemistry 41 2002 15296 15303
    • (2002) Biochemistry , vol.41 , pp. 15296-15303
    • Silva, R.A.G.D.1    Nguyen, J.Y.2    Decatur, S.M.3
  • 37
    • 0033973184 scopus 로고    scopus 로고
    • 13C isotope labeling of hydrophobic peptides. Origin of the anomalous intensity distribution in the infrared amide I spectral region of β-sheet structures
    • 13C isotope labeling of hydrophobic peptides. Origin of the anomalous intensity distribution in the infrared amide I spectral region of β-sheet structures J. Am. Chem. Soc. 122 2000 677 683
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 677-683
    • Brauner, J.W.1    Dugan, C.2    Mendelsohn, R.3
  • 38
    • 2442540096 scopus 로고    scopus 로고
    • Vibrational coupling, isotope editing, and β-sheet structure in a membrane-bound polypeptide
    • C. Paul, J. Wang, W.C. Wimley, R.M. Hochstrasser, and P.H. Axelsen Vibrational coupling, isotope editing, and β-sheet structure in a membrane-bound polypeptide J. Am. Chem. Soc. 126 2004 5843 5850
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5843-5850
    • Paul, C.1    Wang, J.2    Wimley, W.C.3    Hochstrasser, R.M.4    Axelsen, P.H.5
  • 40
    • 17744395315 scopus 로고    scopus 로고
    • β sheet structure in amyloid beta fibrils and vibrational dipolar coupling
    • C. Paul, and P.H. Axelsen β sheet structure in amyloid beta fibrils and vibrational dipolar coupling J. Am. Chem. Soc. 127 2005 5754 5755
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5754-5755
    • Paul, C.1    Axelsen, P.H.2
  • 41
    • 0030832914 scopus 로고    scopus 로고
    • Structural coupling between the oxygen-evolving Mn cluster and a tyrosine residue in photosystem II as revealed by Fourier transform infrared spectroscopy
    • T. Noguchi, Y. Inoue, and X.-S. Tang Structural coupling between the oxygen-evolving Mn cluster and a tyrosine residue in photosystem II as revealed by Fourier transform infrared spectroscopy Biochemstry 36 1997 14705 14711
    • (1997) Biochemstry , vol.36 , pp. 14705-14711
    • Noguchi, T.1    Inoue, Y.2    Tang, X.-S.3
  • 42
    • 0030734034 scopus 로고    scopus 로고
    • Fourier transform infrared difference spectroscopy of photosystem II tyrosine D using site-directed mutagenesis and specific isotope labeling
    • R. Hienerwadel, A. Boussac, J. Breton, B.A. Diner, and C. Berthomieu Fourier transform infrared difference spectroscopy of photosystem II tyrosine D using site-directed mutagenesis and specific isotope labeling Biochemistry 36 1997 14712 14723
    • (1997) Biochemistry , vol.36 , pp. 14712-14723
    • Hienerwadel, R.1    Boussac, A.2    Breton, J.3    Diner, B.A.4    Berthomieu, C.5
  • 43
    • 0035799325 scopus 로고    scopus 로고
    • Vibrational structure of GDP and GTP bound to RAS: An isotope-edited FTIR study
    • H. Cheng, S. Sukal, H. Deng, T.S. Leyh, and R. Callender Vibrational structure of GDP and GTP bound to RAS: an isotope-edited FTIR study Biochemistry 40 2001 4035 4043
    • (2001) Biochemistry , vol.40 , pp. 4035-4043
    • Cheng, H.1    Sukal, S.2    Deng, H.3    Leyh, T.S.4    Callender, R.5
  • 44
    • 4744367356 scopus 로고    scopus 로고
    • Linear dichroism of biomolecules: Which way is up?
    • T.R. Dafforn, and A. Rodger Linear dichroism of biomolecules: which way is up? Curr. Opin. Struct. Biol. 14 2004 541 546
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 541-546
    • Dafforn, T.R.1    Rodger, A.2
  • 45
    • 0028086944 scopus 로고
    • Determination of CO orientation in myoglobin by single-crystal infrared linear dichroism
    • D. Ivanov, J.T. Sage, M. Keim, J.R. Powell, S.A. Asher, and P.M. Champion Determination of CO orientation in myoglobin by single-crystal infrared linear dichroism J. Am. Chem. Soc. 116 1994 4139 4140
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4139-4140
    • Ivanov, D.1    Sage, J.T.2    Keim, M.3    Powell, J.R.4    Asher, S.A.5    Champion, P.M.6
  • 46
    • 0030681044 scopus 로고    scopus 로고
    • Structural characterization of the myoglobin active site using infrared crystallography
    • J.T. Sage, and W. Jee Structural characterization of the myoglobin active site using infrared crystallography J. Mol. Biol. 274 1997 21 26
    • (1997) J. Mol. Biol. , vol.274 , pp. 21-26
    • Sage, J.T.1    Jee, W.2
  • 47
    • 0029933595 scopus 로고    scopus 로고
    • Isotope-edited infrared linear dichroism: Determination of amide orientational relationships
    • T.S. Anderson, J. Hellgeth, and P.T. Lansbury Jr. Isotope-edited infrared linear dichroism: determination of amide orientational relationships J. Am. Chem. Soc. 118 1996 6540 6546
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6540-6546
    • Anderson, T.S.1    Hellgeth, J.2    Lansbury Jr., P.T.3
  • 48
    • 0035143368 scopus 로고    scopus 로고
    • FTIR microscopic imaging of collagen and proteoglycan in bovine cartilage
    • N.P. Camacho, P. West, P.A. Torzilli, and R. Mendelsohn FTIR microscopic imaging of collagen and proteoglycan in bovine cartilage Biopolymers 62 2001 1 8
    • (2001) Biopolymers , vol.62 , pp. 1-8
    • Camacho, N.P.1    West, P.2    Torzilli, P.A.3    Mendelsohn, R.4
  • 49
    • 0001397162 scopus 로고    scopus 로고
    • Discordant results on FeCO deformability in Heme proteins reconciled by density functional theory
    • T.G. Spiro, and P.M. Kozlowski Discordant results on FeCO deformability in Heme proteins reconciled by density functional theory J. Am. Chem. Soc. 120 1998 4524 4525
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4524-4525
    • Spiro, T.G.1    Kozlowski, P.M.2
  • 50
    • 0035110522 scopus 로고    scopus 로고
    • Is the CO adduct of myoglobin bent, and does it matter?
    • T.G. Spiro, and P.M. Kozlowski Is the CO adduct of myoglobin bent, and does it matter? Acc. Chem. Res. 34 2001 137 144
    • (2001) Acc. Chem. Res. , vol.34 , pp. 137-144
    • Spiro, T.G.1    Kozlowski, P.M.2
  • 51
    • 0030628997 scopus 로고    scopus 로고
    • Infrared and Raman vibrational optical activity: Theoretical and experimental aspects
    • L.A. Nafie Infrared and Raman vibrational optical activity: theoretical and experimental aspects Annu. Rev. Phys. Chem. 48 1997 357 386
    • (1997) Annu. Rev. Phys. Chem. , vol.48 , pp. 357-386
    • Nafie, L.A.1
  • 52
    • 0036802313 scopus 로고    scopus 로고
    • Protein and peptide secondary structure and conformational determination with vibrational circular dichroism
    • T.A. Keiderling Protein and peptide secondary structure and conformational determination with vibrational circular dichroism Curr. Opin. Chem. Biol. 6 2002 682 688
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 682-688
    • Keiderling, T.A.1
  • 54
    • 0037961802 scopus 로고    scopus 로고
    • Time-resolved Fourier transform infrared spectroscopic imaging
    • R. Bhargava, and I.W. Levin Time-resolved Fourier transform infrared spectroscopic imaging Appl. Spectrosc. 57 2003 357 366
    • (2003) Appl. Spectrosc. , vol.57 , pp. 357-366
    • Bhargava, R.1    Levin, I.W.2
  • 55
    • 21244464637 scopus 로고    scopus 로고
    • Fourier transform infrared vibrational spectroscopic imaging: Integrating microscopy and molecular recognition
    • I.W. Levin, and R. Bhargava Fourier transform infrared vibrational spectroscopic imaging: integrating microscopy and molecular recognition Annu. Rev. Phys. Chem. 56 2005 429 474
    • (2005) Annu. Rev. Phys. Chem. , vol.56 , pp. 429-474
    • Levin, I.W.1    Bhargava, R.2
  • 56
    • 1642297346 scopus 로고    scopus 로고
    • Core structure of amyloid fibril proposed from IR-microscope linear dichroism
    • H. Hiramatsu, Y. Goto, H. Naiki, and T. Kitagawa Core structure of amyloid fibril proposed from IR-microscope linear dichroism J. Am. Chem. Soc. 126 2004 3008 3009
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3008-3009
    • Hiramatsu, H.1    Goto, Y.2    Naiki, H.3    Kitagawa, T.4
  • 57
    • 0041190599 scopus 로고
    • The interpretation of infrared dichroism in fibrous protein structures
    • R.D.B. Fraser The interpretation of infrared dichroism in fibrous protein structures J. Chem. Phys. 21 1953 1511 1515
    • (1953) J. Chem. Phys. , vol.21 , pp. 1511-1515
    • Fraser, R.D.B.1
  • 58
    • 0026549587 scopus 로고
    • Exploiting stopped-flow injection methods for quantitative chemical-assays
    • G.D. Christian, and J. Ruzicka Exploiting stopped-flow injection methods for quantitative chemical-assays Anal. Chim. Acta 261 1992 11 21
    • (1992) Anal. Chim. Acta , vol.261 , pp. 11-21
    • Christian, G.D.1    Ruzicka, J.2
  • 62
    • 0032870911 scopus 로고    scopus 로고
    • Stable isotope-labeled peptides in study of protein aggregation
    • M.A. Baldwin Stable isotope-labeled peptides in study of protein aggregation Methods Enzymol. 309 1999 576 591
    • (1999) Methods Enzymol. , vol.309 , pp. 576-591
    • Baldwin, M.A.1
  • 63
    • 0242490659 scopus 로고    scopus 로고
    • The organization and assembly of a β-sheet formed by a prion peptide in solution: An isotope-edited FTIR study
    • R.A.G.D. Silva, W. Barber-Armstrong, and S.M. Decatur The organization and assembly of a β-sheet formed by a prion peptide in solution: an isotope-edited FTIR study J. Am. Chem. Soc. 125 2003 13674 13675
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13674-13675
    • Silva, R.A.G.D.1    Barber-Armstrong, W.2    Decatur, S.M.3
  • 66
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases
    • M.F. Perutz, T. Johnson, M. Suzuki, and J.T. Finch Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases Proc. Natl. Acad. Sci. U. S. A. 91 1994 5355 5358
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 68
    • 3142699791 scopus 로고    scopus 로고
    • Template-assisted filament growth by parallel stacking of tau
    • M. Margittai, and R. Langen Template-assisted filament growth by parallel stacking of tau Proc. Natl. Acad. Sci. U. S. A. 101 2004 10278 10283
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10278-10283
    • Margittai, M.1    Langen, R.2
  • 70
    • 0034076545 scopus 로고    scopus 로고
    • Do parallel β-helix proteins have a unique Fourier transform infrared spectrum?
    • R. Khurana, and A.L. Fink Do parallel β-helix proteins have a unique Fourier transform infrared spectrum? Biophys. J. 78 2000 994 1000
    • (2000) Biophys. J. , vol.78 , pp. 994-1000
    • Khurana, R.1    Fink, A.L.2
  • 71
    • 15244356060 scopus 로고    scopus 로고
    • High hydrostatic pressure dissociates early aggregates of TTR105-115, but not the mature amyloid fibrils
    • C. Dirix, F. Meersman, C.E. MacPhee, C.M. Dobson, and K. Heremans High hydrostatic pressure dissociates early aggregates of TTR105-115, but not the mature amyloid fibrils J. Mol. Biol. 347 2005 903 909
    • (2005) J. Mol. Biol. , vol.347 , pp. 903-909
    • Dirix, C.1    Meersman, F.2    MacPhee, C.E.3    Dobson, C.M.4    Heremans, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.