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Volumn 81, Issue 1, 2014, Pages 98-106

Investigation of the structure of alpha-lactalbumin protein nanotubes using optical spectroscopy

Author keywords

FTIR; Microscopy; Protein nanotubes; Raman; Lactalbumin

Indexed keywords

BACILLUS LICHENIFORMIS;

EID: 84896546402     PISSN: 00220299     EISSN: 14697629     Source Type: Journal    
DOI: 10.1017/S0022029913000629     Document Type: Article
Times cited : (22)

References (33)
  • 2
    • 0023377695 scopus 로고
    • Thermal denaturation of globular proteins fourier transform-infrared studies of the amide iii spectral region
    • Anderle G & Mendelsohn R 1987 Thermal denaturation of globular proteins Fourier transform-infrared studies of the amide III spectral region. Biophysical Journal 52 69-74
    • (1987) Biophysical Journal , vol.52 , pp. 69-74
    • Anderle, G.1    Mendelsohn, R.2
  • 3
    • 77954219546 scopus 로고    scopus 로고
    • PH-induced conformational transitions in ?-lactalbumin investigated with two-dimensional Raman correlation variance plots and moving windows
    • Ashton L & Blanch EW 2010 pH-induced conformational transitions in ?-lactalbumin investigated with two-dimensional Raman correlation variance plots and moving windows. Journal of Molecular Structure 947 132-138
    • (2010) Journal of Molecular Structure , vol.947 , pp. 132-138
    • Ashton, L.1    Blanch, E.W.2
  • 5
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth A 2007 Infrared spectroscopy of proteins. Biochimica et Biophysica Acta 1767 1073-1101
    • (2007) Biochimica et Biophysica Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 6
    • 0001108755 scopus 로고    scopus 로고
    • Raman optical activity characterization of native and molten globule states of equine lysozyme: Comparison with hen lysozyme and bovine ?-lactalbumin
    • Blanch EW, Morozova-Roche LA, Hecht L, Noppe W & Barron LD 2000 Raman optical activity characterization of native and molten globule states of equine lysozyme: comparison with hen lysozyme and bovine ?-lactalbumin. Biopolymers (Biospectroscopy) 57 235-248
    • (2000) Biopolymers (Biospectroscopy , vol.57 , pp. 235-248
    • Blanch, E.W.1    Morozova-Roche, L.A.2    Hecht, L.3    Noppe, W.4    Barron, L.D.5
  • 7
    • 0026503259 scopus 로고
    • Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching
    • Breddam K & MeldalM1992 Substrate preferences of glutamic-acid- specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching. European Journal of Blochemistry 206 103-107
    • (1992) European Journal of Blochemistry , vol.206 , pp. 103-107
    • Breddam, K.1    Meldal, M.2
  • 9
    • 4043078473 scopus 로고    scopus 로고
    • Influence of calcium on the self-assembly of partially hydrolyzed ?-lactalbumin
    • Graveland-Bikker JF, Ipsen R, Otte J & de Kruif CG 2004 Influence of calcium on the self-assembly of partially hydrolyzed ?-lactalbumin. Langmuir 20 6841-6846
    • (2004) Langmuir , vol.20 , pp. 6841-6846
    • Graveland-Bikker, J.F.1    Ipsen, R.2    Otte, J.3    De Kruif, C.G.4
  • 12
    • 1542299045 scopus 로고    scopus 로고
    • Raman spectroscopy of heat-induced finestranded and particulate ?-lactoglobulin gels
    • Ikeda S & Li-Chan ECY 2004 Raman spectroscopy of heat-induced finestranded and particulate ?-lactoglobulin gels. Food Hydrocolloids 18 489-498
    • (2004) Food Hydrocolloids , vol.18 , pp. 489-498
    • Ikeda, S.1    Li-Chan, E.C.Y.2
  • 13
    • 12344265570 scopus 로고    scopus 로고
    • Nano-structuring by means of proteolysis rheology of novel gels from ?-lactalbumin
    • Ipsen R & Otte J 2003 Nano-structuring by means of proteolysis rheology of novel gels from ?-lactalbumin. Annual Transactions of the Nordic Rheology Society 11 89-93
    • (2003) Annual Transactions of the Nordic Rheology Society , vol.11 , pp. 89-93
    • Ipsen, R.1    Otte, J.2
  • 14
    • 34648834587 scopus 로고    scopus 로고
    • Self-assembly of partially hydrolysed ?-lactalbumin
    • Ipsen R & Otte J 2007 Self-assembly of partially hydrolysed ?-lactalbumin. Biotechnology Advances 25 602-605
    • (2007) Biotechnology Advances , vol.25 , pp. 602-605
    • Ipsen, R.1    Otte, J.2
  • 15
    • 0034914095 scopus 로고    scopus 로고
    • Molecular self-assembly of partially hydrolysed ?-lactalbumin resulting in strong gels with a novel microstructure
    • Ipsen R, Otte J & Qvist KB 2001 Molecular self-assembly of partially hydrolysed ?-lactalbumin resulting in strong gels with a novel microstructure. Journal of Dairy Research 68 277-286
    • (2001) Journal of Dairy Research , vol.68 , pp. 277-286
    • Ipsen, R.1    Otte, J.2    Qvist, K.B.3
  • 16
    • 84896547280 scopus 로고    scopus 로고
    • Protease induced nano-tubular gels from ?-lactalbumin
    • (Eds E Dickinson & T van Vliet). London: Royal Society of Chemistry
    • Ipsen R, Otte J & Qvist KB 2003 Protease induced nano-tubular gels from ?-lactalbumin. In Food Colloids, Biopolymers and Materials, Special Publication, Vol. 284, pp. 84-92 (Eds E Dickinson & T van Vliet). London: Royal Society of Chemistry
    • (2003) Food Colloids, Biopolymers and Materials, Special Publication , vol.284 , pp. 84-92
    • Ipsen, R.1    Otte, J.2    Qvist, K.B.3
  • 18
    • 84985698763 scopus 로고
    • The raman spectra of bence-jones proteins disulfide stretching frequencies and dependence of raman intensity of tryptophan residua on their environments
    • Kitagawa T, Azuma T & Hamaguchi K 1979 The Raman spectra of Bence-Jones proteins. Disulfide stretching frequencies and dependence of Raman intensity of tryptophan residua on their environments. Biopolymers 18 451-465
    • (1979) Biopolymers , vol.18 , pp. 451-465
    • Kitagawa, T.1    Azuma, T.2    Hamaguchi, K.3
  • 19
    • 34548094323 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopic analysis of protein secondary structures
    • Kong J & Yu S 2007 Fourier Transform Infrared Spectroscopic Analysis of protein secondary structures. Acta Biochimica et Biophysica Sinica 39 549-559
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , pp. 549-559
    • Kong, J.1    Yu, S.2
  • 20
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm S & Bandekar J 1986 Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Advanced in Protein Chemistry 38 181-367
    • (1986) Advanced in Protein Chemistry , vol.38 , pp. 181-367
    • Krimm, S.1    Bandekar, J.2
  • 21
    • 0014945047 scopus 로고
    • Laser-excited raman spectroscopy of biomolecules I. Native lysozyme and its constituent amino acids
    • Lord RC & Yu NT 1970 Laser-excited Raman spectroscopy of biomolecules. I. Native lysozyme and its constituent amino acids. Journal of Molecular Biology 50 509-524
    • (1970) Journal of Molecular Biology , vol.50 , pp. 509-524
    • Lord, R.C.1    Yu, N.T.2
  • 23
    • 84988158466 scopus 로고
    • Tryptophan raman bands sensitive to hydrogen bonding and side-chain conformation
    • Miura T, Takeuchi H & Harada I 1989 Tryptophan Raman bands sensitive to hydrogen bonding and side-chain conformation. Journal of Raman Spectroscopy 20 667-671
    • (1989) Journal of Raman Spectroscopy , vol.20 , pp. 667-671
    • Miura, T.1    Takeuchi, H.2    Harada, I.3
  • 24
    • 0030609040 scopus 로고    scopus 로고
    • FT-IR study of the Ca2+-binding to bovine ?-lactalbumin
    • Mizuguchi M, Nara M, Kawano K & Nitta K 1997 FT-IR study of the Ca2+-binding to bovine ?-lactalbumin. FEBS Letters 417 153-156
    • (1997) FEBS Letters , vol.417 , pp. 153-156
    • Mizuguchi, M.1    Nara, M.2    Kawano, K.3    Nitta, K.4
  • 25
    • 0016302856 scopus 로고
    • Conformation of the cystine linkages in bovine ?-lactalbumin as revealed by its Raman effect
    • Nakanishi M, Takesada H & Tsuboi M 1974 Conformation of the cystine linkages in bovine ?-lactalbumin as revealed by its Raman effect. Journal of Molecular Biology 89 241-243
    • (1974) Journal of Molecular Biology , vol.89 , pp. 241-243
    • Nakanishi, M.1    Takesada, H.2    Tsuboi, M.3
  • 27
  • 28
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • Rajagapol K & Schneider JP 2004 Self-assembling peptides and proteins for nanotechnological applications. Current Opinion in Structural Biology 14 480-486
    • (2004) Current Opinion in Structural Biology , vol.14 , pp. 480-486
    • Rajagapol, K.1    Schneider, J.P.2
  • 29
    • 0021811195 scopus 로고
    • Ultraviolet resonance Raman spectra of insulin and ?-lactalbumin with 218-and 200-nm laser excitation
    • Rava RP & Spiro TG 1984 Ultraviolet resonance Raman spectra of insulin and ?-lactalbumin with 218-and 200-nm laser excitation. Biochemistry 24 1861-1865
    • (1984) Biochemistry , vol.24 , pp. 1861-1865
    • Rava, R.P.1    Spiro, T.G.2
  • 30
    • 0017340687 scopus 로고
    • Laser Raman scattering as a probe of protein structure
    • Spiro TG & Gaber BP 1977 Laser Raman scattering as a probe of protein structure. Annual Review of Biochemistry 46 553-572
    • (1977) Annual Review of Biochemistry , vol.46 , pp. 553-572
    • Spiro, T.G.1    Gaber, B.P.2
  • 31
    • 0002660213 scopus 로고
    • Peptide backbone conformation and microenvironment of protein side chains in spectroscopy of biological systems
    • (Eds Clark RJH & Haster RE) New York: John Wiley & Sons
    • Tu AT 1986 Peptide backbone conformation and microenvironment of protein side chains in spectroscopy of biological systems In: Spectroscopy of Biological Systems, pp. 47-112 (Eds Clark RJH & Haster RE) New York: John Wiley & Sons
    • (1986) Spectroscopy of Biological Systems , pp. 47-112
    • Tu, A.T.1
  • 32
    • 0029585995 scopus 로고
    • Vibrational raman optical activity of alpha-lactalbumin: Comparison with lysozyme, and evidence for native tertiary folds in molten globule states
    • Wilson G, Ford SJ, Cooper A, Hecht L, Wen ZQ & Barron LD 1995 Vibrational Raman optical activity of alpha-lactalbumin: comparison with lysozyme, and evidence for native tertiary folds in molten globule states. Journal of Molecular Biology 254 747-760
    • (1995) Journal of Molecular Biology , vol.254 , pp. 747-760
    • Wilson, G.1    Ford, S.J.2    Cooper, A.3    Hecht, L.4    Wen, Z.Q.5    Barron, L.D.6
  • 33
    • 0037315181 scopus 로고    scopus 로고
    • Studies on amide III infrared bands for the secondary structure determination of proteins
    • Xie M-X & Liu Y 2003 Studies on amide III infrared bands for the secondary structure determination of proteins. Chemical Journal of Chinese Universities 24 226-231
    • (2003) Chemical Journal of Chinese Universities , vol.24 , pp. 226-231
    • Xie, M.-X.1    Liu, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.