메뉴 건너뛰기




Volumn 78, Issue 2, 2000, Pages 994-1000

Do parallel β-helix proteins have a unique Fourier transform infrared spectrum?

Author keywords

[No Author keywords available]

Indexed keywords

POLYPEPTIDE;

EID: 0034076545     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76657-4     Document Type: Article
Times cited : (114)

References (41)
  • 1
    • 84996082984 scopus 로고
    • Normal mode spectrum of the parallel-chain β-sheet
    • Bandekar, J., and S. Krimm. 1988. Normal mode spectrum of the parallel-chain β-sheet. Biopolymers. 27:909-921.
    • (1988) Biopolymers. , vol.27 , pp. 909-921
    • Bandekar, J.1    Krimm, S.2
  • 2
    • 0028130122 scopus 로고
    • Interfacial adsorption and aggregation associated changes in secondary structure of human calcitonin monitored by ATR-FT-IR spectroscopy
    • Bauer, H. H., M. Muller. J. Goette, H. P. Merkle, and U. P. Fringeli. 1994. Interfacial adsorption and aggregation associated changes in secondary structure of human calcitonin monitored by ATR-FT-IR spectroscopy. Biochemistry. 33:12276-12282.
    • (1994) Biochemistry. , vol.33 , pp. 12276-12282
    • Bauer, H.H.1    Muller, M.2    Goette, J.3    Merkle, H.P.4    Fringeli, U.P.5
  • 3
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • Baumann, U., S. Wu, K. M. Flaherty, and D. B. McKay. 1993. Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 12:3357-3364.
    • (1993) EMBO J. , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 5
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D. M., and H. Susi. 1986. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers. 25:469-487.
    • (1986) Biopolymers. , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 6
    • 0030997806 scopus 로고    scopus 로고
    • Secondary structures comparison of aquaporin-1 and bacteriorhodopsin: A Fourier transform infrared spectroscopy study of two-dimensional membrane crystals
    • Cabiaux, V., K. A. Oberg, P. Pancoska, T. Walz, P. Agre, and A. Engel. 1997. Secondary structures comparison of aquaporin-1 and bacteriorhodopsin: a Fourier transform infrared spectroscopy study of two-dimensional membrane crystals. Biophys. J. 73:406-417.
    • (1997) Biophys. J. , vol.73 , pp. 406-417
    • Cabiaux, V.1    Oberg, K.A.2    Pancoska, P.3    Walz, T.4    Agre, P.5    Engel, A.6
  • 7
    • 0024386063 scopus 로고
    • The secondary structure of human amyloid deposits as determined by circular dichroism spectroscopy
    • Cascio, M., P. A. Glazer, and B. A. Wallace. 1989. The secondary structure of human amyloid deposits as determined by circular dichroism spectroscopy. Biochem. Biophys. Res. Commun. 162:1162-1166.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 1162-1166
    • Cascio, M.1    Glazer, P.A.2    Wallace, B.A.3
  • 8
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey, B. W., A. Dong, K. S. Bhat, D. Ernst, S. F. Hayes, and W. S. Caughey. 1991. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry. 30:7672-7680.
    • (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
  • 9
    • 0030298195 scopus 로고    scopus 로고
    • The different molar absorptivities of the secondary structure types in the amide I region: An attenuated total reflection infrared study on globular proteins
    • de Jongh, H. H., E. Goormaghtigh, and J. M. Ruysschaert. 1996. The different molar absorptivities of the secondary structure types in the amide I region: an attenuated total reflection infrared study on globular proteins. Anal. Biochem. 242:95-103.
    • (1996) Anal. Biochem. , vol.242 , pp. 95-103
    • Jongh, H.H.1    Goormaghtigh, E.2    Ruysschaert, J.M.3
  • 10
    • 0025357111 scopus 로고
    • Protein secondary structures in water from 2nd-derivative amide-I infrared spectra
    • Dong, A., P. Huang, and W. S. Caughey. 1990. Protein secondary structures in water from 2nd-derivative amide-I infrared spectra. Biochemistry. 29:3303-3308.
    • (1990) Biochemistry. , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 11
    • 0028916150 scopus 로고
    • Infrared spectroscopic studies of lyophilization-and temperature-induced protein aggregation
    • Dong, A. C., S. J. Prestrelski, S. D. Allison, and J. F. Carpenter. 1995. Infrared spectroscopic studies of lyophilization-and temperature-induced protein aggregation. J. Pharm. Sci. 84:415-424.
    • (1995) J. Pharm. Sci. , vol.84 , pp. 415-424
    • Dong, A.C.1    Prestrelski, S.J.2    Allison, S.D.3    Carpenter, J.F.4
  • 12
    • 0028864109 scopus 로고
    • Molecular modeling indicates that homodimers form the basis for intermediate filament assembly from human and mouse epidermal keratins
    • Downing, D. T. 1995. Molecular modeling indicates that homodimers form the basis for intermediate filament assembly from human and mouse epidermal keratins. Proteins. 23:204-217.
    • (1995) Proteins. , vol.23 , pp. 204-217
    • Downing, D.T.1
  • 13
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley, P., I. G. Charles, N. F. Fairweather, and N. W. Isaacs. 1996. Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature. 381:90-92.
    • (1996) Nature. , vol.381 , pp. 90-92
    • Emsley, P.1    Charles, I.G.2    Fairweather, N.F.3    Isaacs, N.W.4
  • 14
    • 0031933289 scopus 로고    scopus 로고
    • Discrete intermediates vs. Molten globule models of protein folding: Characterization of partially-folded intermediates of apomyoglobin
    • Fink, A. L., K. A. Oberg, and S. Seshadri. 1997. Discrete intermediates vs. molten globule models of protein folding: characterization of partially-folded intermediates of apomyoglobin. Folding and Design. 3:19-25.
    • (1997) Folding and Design. , vol.3 , pp. 19-25
    • Fink, A.L.1    Oberg, K.A.2    Seshadri, S.3
  • 15
    • 0003979510 scopus 로고    scopus 로고
    • Determination of secondary structure in protein aggregates using attenuated total reflectance (ATR) FTIR
    • B. R. Singh, editor. American Chemical Society, New York
    • Fink, A. L., S. Seshadri, R. Khurana, and K. A. Oberg. 1999. Determination of secondary structure in protein aggregates using attenuated total reflectance (ATR) FTIR. In Infrared Analysis of Peptides and Proteins. B. R. Singh, editor. American Chemical Society, New York.
    • (1999) Infrared Analysis of Peptides and Proteins
    • Fink, A.L.1    Seshadri, S.2    Khurana, R.3    Oberg, K.A.4
  • 16
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films
    • Goormaghtigh, E., V. Cabiaux, and J. M. Ruysschaert. 1990. Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. Eur. J. Biochem. 193:409-420.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.M.3
  • 17
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh, E., V. Raussens, and J. M. Ruysschaert. 1999. Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim. Biophys. Acta. 1422:105-185.
    • (1999) Biochim. Biophys. Acta. , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.M.3
  • 19
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M., and H. H. Mantsch. 1995. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30:95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 20
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C., Jr. 1990. Protein secondary structure and circular dichroism: a practical guide. Proteins. 7:205-214.
    • (1990) Proteins. , vol.7 , pp. 205-214
    • Johnson W.C., Jr.1
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structure
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24:946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 22
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S., and J. Bandekar. 1986. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38:181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 23
    • 0024281641 scopus 로고
    • Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A
    • Langs, D. A. 1988. Three-dimensional structure at 0.86 Å of the uncomplexed form of the transmembrane ion channel peptide gramicidin A. Science. 241:188-191.
    • (1988) Science. , vol.241 , pp. 188-191
    • Langs, D.A.1
  • 25
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from β-helical protofibrils
    • Lazo, N. D., and D. T. Downing. 1998. Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry. 37:1731-1735.
    • (1998) Biochemistry. , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Downing, D.T.2
  • 26
    • 0024999461 scopus 로고
    • Determination of protein secondary structure using factor analysis of infrared spectra
    • Lee, D. C., P. I. Haris, D. Chapman, and R. C. Mitchell. 1990. Determination of protein secondary structure using factor analysis of infrared spectra. Biochemistry. 29:9185-9193.
    • (1990) Biochemistry. , vol.29 , pp. 9185-9193
    • Lee, D.C.1    Haris, P.I.2    Chapman, D.3    Mitchell, R.C.4
  • 27
    • 0024826939 scopus 로고
    • Underlying assumptions in the estimation of secondary structure content
    • Manning, M. C. 1989. Underlying assumptions in the estimation of secondary structure content. J. Pharm. Biomed. Anal. 7:1103-1119.
    • (1989) J. Pharm. Biomed. Anal. , vol.7 , pp. 1103-1119
    • Manning, M.C.1
  • 28
    • 0024065282 scopus 로고
    • Circular dichroism studies of distorted alpha-helices, twisted beta-sheets, and beta turns
    • Manning, M. C., M. Illangasekare, and R. W. Woody. 1988. Circular dichroism studies of distorted alpha-helices, twisted beta-sheets, and beta turns. Biophys. Chem. 31:77-86.
    • (1988) Biophys. Chem. , vol.31 , pp. 77-86
    • Manning, M.C.1    Illangasekare, M.2    Woody, R.W.3
  • 29
    • 0022534327 scopus 로고
    • Vibrational analysis of the structure of gramicidin A. II. Vibrational spectra
    • Naik, V. M., and S. Krimm. 1986. Vibrational analysis of the structure of gramicidin A. II. Vibrational spectra. Biophys. J. 49:1147-1154.
    • (1986) Biophys. J. , vol.49 , pp. 1147-1154
    • Naik, V.M.1    Krimm, S.2
  • 30
    • 0043106211 scopus 로고
    • Methods for collecting and analyzing attenuated total reflectance FTIR spectra of proteins in solution
    • W. Crabb, editor. Academic Press, San Diego.
    • Oberg, K. A., and A. L. Fink. 1995. Methods for collecting and analyzing attenuated total reflectance FTIR spectra of proteins in solution. In Techniques in Protein Chemistry. W. Crabb, editor. Academic Press, San Diego. 475-484.
    • (1995) Techniques in Protein Chemistry , pp. 475-484
    • Oberg, K.A.1    Fink, A.L.2
  • 31
    • 0032005382 scopus 로고    scopus 로고
    • A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution
    • Oberg, K. A., and A. L. Fink. 1998. A new attenuated total reflectance Fourier transform infrared spectroscopy method for the study of proteins in solution. Anal. Biochem. 256:92-106.
    • (1998) Anal. Biochem. , vol.256 , pp. 92-106
    • Oberg, K.A.1    Fink, A.L.2
  • 32
    • 0031569829 scopus 로고    scopus 로고
    • The crystal structure of rhamnogalacturonase A from Aspergillus
    • Petersen, T. N., S. Kauppinen, and S. Larsen. 1997. The crystal structure of rhamnogalacturonase A from Aspergillus. Structure. 5:533-544.
    • (1997) Structure. , vol.5 , pp. 533-544
    • Petersen, T.N.1    Kauppinen, S.2    Larsen, S.3
  • 33
    • 0028844306 scopus 로고
    • A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz, C. R., and S. L. Roderick. 1995. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science. 270: 997-1000.
    • (1995) Science. , vol.270 , pp. 997-1000
    • Raetz, C.R.1    Roderick, S.L.2
  • 34
    • 0029081224 scopus 로고
    • Circular dichroism of the parallel β-helical proteins pectate lyase C and E
    • Sieber, V., F. Jurnak, and G. R. Moe. 1995. Circular dichroism of the parallel β-helical proteins pectate lyase C and E. Proteins Struct. Funct. Genet. 23:32-37.
    • (1995) Proteins Struct. Funct. Genet. , vol.23 , pp. 32-37
    • Sieber, V.1    Jurnak, F.2    Moe, G.R.3
  • 35
    • 0028095571 scopus 로고
    • Crystal structure of P22 tailspike protein: Interdigitated subunits in a thermostable trimer
    • Steinbacher, S., R. Seckler, S. Miller, B. Steipe, R. Huber, and P. Reinemer. 1994. Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. Science. 265:383-386.
    • (1994) Science. , vol.265 , pp. 383-386
    • Steinbacher, S.1    Seckler, R.2    Miller, S.3    Steipe, B.4    Huber, R.5    Reinemer, P.6
  • 36
    • 0023442501 scopus 로고
    • Fourier transform infrared study of proteins with parallel beta-chains
    • Susi, H., and D. M. Byler. 1987. Fourier transform infrared study of proteins with parallel beta-chains. Arch. Biochem. Biophys. 258: 465-469.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 465-469
    • Susi, H.1    Byler, D.M.2
  • 37
    • 0030744878 scopus 로고    scopus 로고
    • X-ray diffraction and far-UV CD studies of filaments formed by a leucine-rich repeat peptide: Structural similarity to the amyloid fibrils of prions and Alzheimer's disease beta-protein
    • Symmons, M. F., S. G. Buchanan, D. T. Clarke, G. Jones, and N. J. Gay. 1997. X-ray diffraction and far-UV CD studies of filaments formed by a leucine-rich repeat peptide: structural similarity to the amyloid fibrils of prions and Alzheimer's disease beta-protein. FEBS Lett. 412: 397-403.
    • (1997) FEBS Lett. , vol.412 , pp. 397-403
    • Symmons, M.F.1    Buchanan, S.G.2    Clarke, D.T.3    Jones, G.4    Gay, N.J.5
  • 39
    • 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: 1243-1257.
    • (1990) Biopolymers. , vol.30 , pp. 1243-1257
    • Venyaminov, S.Y.1    Kalnin, N.N.2
  • 40
    • 0024281633 scopus 로고
    • The gramicidin pore: Crystal structure of a cesium complex
    • Wallace, B. A., and K. Ravikumar. 1988. The gramicidin pore: crystal structure of a cesium complex. Science. 241:182-187.
    • (1988) Science. , vol.241 , pp. 182-187
    • Wallace, B.A.1    Ravikumar, K.2
  • 41
    • 0027329090 scopus 로고
    • New domain motif: The structure of pectate lyase C, a secreted plant virulence factor
    • Yoder, M. D., N. T. Keen, and F. Jurnak. 1993. New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science. 260:1503-1507.
    • (1993) Science. , vol.260 , pp. 1503-1507
    • Yoder, M.D.1    Keen, N.T.2    Jurnak, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.