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Volumn 64, Issue 3, 1997, Pages 377-397

Solution conformation of a peptide corresponding to bovine κ-casein B residues 130-153 by circular dichroism spectroscopy and 1H-nuclear magnetic resonance spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

BOVINAE; CAPRA HIRCUS; OVIS ARIES; SUS SCROFA; VISCUM ALBUM;

EID: 0031201781     PISSN: 00220299     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0022029997002239     Document Type: Article
Times cited : (22)

References (49)
  • 2
    • 5144229966 scopus 로고
    • Practical aspects of two-dimensional transverse NOE spectroscopy
    • BAX, A. & DAVIS, D. G. 1985 Practical aspects of two-dimensional transverse NOE spectroscopy. Journal of Magnetic Resonance 63 207-213
    • (1985) Journal of Magnetic Resonance , vol.63 , pp. 207-213
    • Bax, A.1    Davis, D.G.2
  • 3
    • 48549112001 scopus 로고
    • Selection of coherence-transfer pathways in NMR pulse experiments
    • BODENHAUSEN, G., KOGLER, H. & ERNST, R. R. 1984 Selection of coherence-transfer pathways in NMR pulse experiments. Journal of Magnetic Resonance 58 370-388
    • (1984) Journal of Magnetic Resonance , vol.58 , pp. 370-388
    • Bodenhausen, G.1    Kogler, H.2    Ernst, R.R.3
  • 5
    • 0025119481 scopus 로고
    • Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance
    • BRADLEY, E. K., THOMASON, J. F., COHEN, F. E., KOSEN, P. A. & KUNTZ, I. D. 1990 Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance. Journal of Molecular Biology 215 607-622
    • (1990) Journal of Molecular Biology , vol.215 , pp. 607-622
    • Bradley, E.K.1    Thomason, J.F.2    Cohen, F.E.3    Kosen, P.A.4    Kuntz, I.D.5
  • 6
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing. Application to proton correlation spectroscopy
    • BRAUNSCHWEILER, L. & ERNST, R. R. 1983 Coherence transfer by isotropic mixing. Application to proton correlation spectroscopy. Journal of Magnetic Resonance 53 521-528
    • (1983) Journal of Magnetic Resonance , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 7
    • 0022412886 scopus 로고
    • Preparation and amino acid sequence of human κ-casein
    • BRIGNON, G., CHTOUROU, A. & RIBADEAU-DUMAS, B. 1985 Preparation and amino acid sequence of human κ-casein. FEBS Letters 188 48-54
    • (1985) FEBS Letters , vol.188 , pp. 48-54
    • Brignon, G.1    Chtourou, A.2    Ribadeau-Dumas, B.3
  • 8
    • 0000942193 scopus 로고
    • Infrared spectroscopic evidence for calcium ion interaction with carboxylate groups of casein
    • BYLER, D. M. & FARRELL, H. M. 1989 Infrared spectroscopic evidence for calcium ion interaction with carboxylate groups of casein. Journal of Dairy Science 72 1719-1723
    • (1989) Journal of Dairy Science , vol.72 , pp. 1719-1723
    • Byler, D.M.1    Farrell, H.M.2
  • 9
    • 0016169865 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • CHEN, Y.-H., YANG, J. T. & CHAU, K. H. 1974 Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 13 3350-3359
    • (1974) Biochemistry , vol.13 , pp. 3350-3359
    • Chen, Y.-H.1    Yang, J.T.2    Chau, K.H.3
  • 10
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins
    • CHOU, P. Y. & FASMAN, G. D. 1974a Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins. Biochemistry 13 211-222
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 11
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • CHOU, P. Y. & FASMAN, G. D. 1974b Prediction of protein conformation. Biochemistry 13 222-245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 12
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • CHOU, P. Y. & FASMAN, G. D. 1978 Prediction of the secondary structure of proteins from their amino acid sequence. Advances in Enzymology 47 45-148
    • (1978) Advances in Enzymology , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 19
    • 0017873321 scopus 로고
    • Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins
    • GARNIER, J., OSGUTHORPE, D. J. & ROBSON, B. 1978 Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. Journal of Molecular Biology 120 97-120
    • (1978) Journal of Molecular Biology , vol.120 , pp. 97-120
    • Garnier, J.1    Osguthorpe, D.J.2    Robson, B.3
  • 20
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • GREENFIELD, N. & FASMAN, G. D. 1969 Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry 8 4108-4116
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 24
    • 0023689754 scopus 로고
    • Primary and predicted secondary structures of the caseins in relation to their biological functions
    • HOLT, C. & SAWYER, L. 1988 Primary and predicted secondary structures of the caseins in relation to their biological functions. Protein Engineering 2 251-259
    • (1988) Protein Engineering , vol.2 , pp. 251-259
    • Holt, C.1    Sawyer, L.2
  • 25
    • 84954920673 scopus 로고
    • Attachment sites of carbohydrate moieties to peptide chain of bovine κ-casein from normal milk
    • KANAMORI, M., KAWAGUCHI, N., IBUKI, F. & DOI, H. 1980 Attachment sites of carbohydrate moieties to peptide chain of bovine κ-casein from normal milk. Agricultural and Biological Chemistry 44 1855-1861
    • (1980) Agricultural and Biological Chemistry , vol.44 , pp. 1855-1861
    • Kanamori, M.1    Kawaguchi, N.2    Ibuki, F.3    Doi, H.4
  • 26
    • 21144479431 scopus 로고
    • Determination of κ-casein glycomacropeptide by high performance liquid chromatography without trichloroacetic acid pretreatment
    • KAWAKAMI, H., KAWASAKI, Y., DOSAKO, S., TANIMOTO, M. & NAKAJIMA, I. 1992 Determination of κ-casein glycomacropeptide by high performance liquid chromatography without trichloroacetic acid pretreatment. Milchwissenschaft 47 688-693
    • (1992) Milchwissenschaft , vol.47 , pp. 688-693
    • Kawakami, H.1    Kawasaki, Y.2    Dosako, S.3    Tanimoto, M.4    Nakajima, I.5
  • 27
    • 0026216795 scopus 로고
    • Three-dimensional molecular modeling of bovine caseins: κ-casein
    • KUMOSINSKI, T. F., BROWN, E. M. & FARRELL, H. M. 1991 Three-dimensional molecular modeling of bovine caseins: κ-casein. Journal of Dairy Science 74 2879-2887
    • (1991) Journal of Dairy Science , vol.74 , pp. 2879-2887
    • Kumosinski, T.F.1    Brown, E.M.2    Farrell, H.M.3
  • 31
    • 85033141110 scopus 로고    scopus 로고
    • LUTTKE, A. 1990a PLOT.A/GOR Koln, Germany
    • LUTTKE, A. 1990a PLOT.A/GOR Koln, Germany
  • 32
    • 85033148505 scopus 로고    scopus 로고
    • LUTTKE, A. 1990b PLOT.A/HEL, Koln, Germany
    • LUTTKE, A. 1990b PLOT.A/HEL, Koln, Germany
  • 33
    • 0028085957 scopus 로고
    • Conformation of a peptide corresponding to T4 lysozyme residues 59-81 by NMR and CD spectroscopy
    • McLEISH, M. J., NIELSEN, K. J., NAJBAR, L. V., WADE, J. D., LIN, F., DOUGHTY, M. B. & CRAIK, D. J. 1994 Conformation of a peptide corresponding to T4 lysozyme residues 59-81 by NMR and CD spectroscopy. Biochemistry 33 11174-11183
    • (1994) Biochemistry , vol.33 , pp. 11174-11183
    • McLeish, M.J.1    Nielsen, K.J.2    Najbar, L.V.3    Wade, J.D.4    Lin, F.5    Doughty, M.B.6    Craik, D.J.7
  • 35
    • 0017049350 scopus 로고
    • Comparative study of the amino acid sequences of the caseinomacropeptides from several species
    • MERCIER, J.-C., CHOBERT, J.-M. & ADDEO, F. 1976 Comparative study of the amino acid sequences of the caseinomacropeptides from several species. FEBS Letters 72 208-214
    • (1976) FEBS Letters , vol.72 , pp. 208-214
    • Mercier, J.-C.1    Chobert, J.-M.2    Addeo, F.3
  • 36
    • 0028921182 scopus 로고
    • 10-helix along the thermodynamic folding pathway
    • 10-helix along the thermodynamic folding pathway. Biochemistry 34 3873-3877
    • (1995) Biochemistry , vol.34 , pp. 3873-3877
    • Millhauser, G.L.1
  • 37
    • 0023096760 scopus 로고
    • Comparison of conformations of κ-casein, para-κ-casein and glycomacropeptide
    • ONO, T., YADA, R., YUTANI, K. & NAKAI, S. 1987 Comparison of conformations of κ-casein, para-κ-casein and glycomacropeptide. Biochimica et Biophysica Acta 911 318-325
    • (1987) Biochimica et Biophysica Acta , vol.911 , pp. 318-325
    • Ono, T.1    Yada, R.2    Yutani, K.3    Nakai, S.4
  • 39
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • PROVENCHER, S. W. & GLÖCKNER, J. 1981 Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20 33-37
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 40
    • 0020595601 scopus 로고
    • Peptide substrates for chymosin (rennin): Conformational studies of κ-casein and some κ-casein-related oligopeptides by circular dichroism and secondary structure prediction
    • RAAP, J., KERLING, K. E. T., VREEMAN, H. J. & VISSER, S. 1983 Peptide substrates for chymosin (rennin): conformational studies of κ-casein and some κ-casein-related oligopeptides by circular dichroism and secondary structure prediction. Archives of Biochemistry and Biophysics 221 117-124
    • (1983) Archives of Biochemistry and Biophysics , vol.221 , pp. 117-124
    • Raap, J.1    Kerling, K.E.T.2    Vreeman, H.J.3    Visser, S.4
  • 41
    • 0029019322 scopus 로고
    • Conformation of two peptides corresponding to human apolipoprotein C-1 residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy
    • ROZEK, A., BUCHKO, G. W. & CUSHLEY, R. J. 1995 Conformation of two peptides corresponding to human apolipoprotein C-1 residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy. Biochemistry 34 7401-7408
    • (1995) Biochemistry , vol.34 , pp. 7401-7408
    • Rozek, A.1    Buchko, G.W.2    Cushley, R.J.3
  • 42
    • 0000492963 scopus 로고
    • Broadband homonuclear cross polarization in 2D N.M.R. using DIPSI-2
    • RUCKER, S. P. & SHAKA, A. J. 1989 Broadband homonuclear cross polarization in 2D N.M.R. using DIPSI-2. Molecular Physics 68 509-517
    • (1989) Molecular Physics , vol.68 , pp. 509-517
    • Rucker, S.P.1    Shaka, A.J.2
  • 43
    • 0026726004 scopus 로고
    • Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide
    • SÖNNICHSEN, F. D., VAN EYK, J. E., HODGES, R. S. & SYKES, B. D. 1992 Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptide. Biochemistry 31 8790-8798
    • (1992) Biochemistry , vol.31 , pp. 8790-8798
    • Sönnichsen, F.D.1    Van Eyk, J.E.2    Hodges, R.S.3    Sykes, B.D.4
  • 44
    • 0024413264 scopus 로고
    • Water-inserted α-helical segments implicate reverse turns as folding intermediates
    • SUNDARALINGAM, M. & SEKHARUDU, Y. C. 1989 Water-inserted α-helical segments implicate reverse turns as folding intermediates. Science 224 1333-1337
    • (1989) Science , vol.224 , pp. 1333-1337
    • Sundaralingam, M.1    Sekharudu, Y.C.2
  • 45
    • 0025858688 scopus 로고
    • Molecular dynamics simulations of the unfolding of an α-helical analogue of ribonuclease A S-peptide in water
    • TIRADO-RIVES, J. & JORGENSEN, W. L. 1991 Molecular dynamics simulations of the unfolding of an α-helical analogue of ribonuclease A S-peptide in water. Biochemistry 30 3864-3871
    • (1991) Biochemistry , vol.30 , pp. 3864-3871
    • Tirado-Rives, J.1    Jorgensen, W.L.2
  • 46
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • WISHART, D. S., SYKES. B. D. & RICHARDS, F. M. 1992 The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31 1647-1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 47
    • 0019871847 scopus 로고
    • Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution
    • WU, C.-S. C., IKEDA, K. & YANG, J. T. 1981 Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry 20 566-570
    • (1981) Biochemistry , vol.20 , pp. 566-570
    • Wu, C.-S.C.1    Ikeda, K.2    Yang, J.T.3


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