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Volumn 71, Issue 2, 1996, Pages 840-847

Fourier-transform infrared spectroscopic studies on avidin secondary structure and complexation with biotin and biotin-lipid assemblies

Author keywords

[No Author keywords available]

Indexed keywords

AVIDIN; BIOTIN;

EID: 0029759030     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79285-8     Document Type: Article
Times cited : (37)

References (34)
  • 1
    • 0024771784 scopus 로고
    • Specific recognition and formation of two-dimensional streptavidin domains in monolayers: Application to molecular devices
    • Ahlers, M., R. Blankenburg, D. W. Grainger, P. Meller, H. Ringsdorf, and C. Salesse. 1989. Specific recognition and formation of two-dimensional streptavidin domains in monolayers: application to molecular devices. Thin Solid Films. 180:93-99.
    • (1989) Thin Solid Films , vol.180 , pp. 93-99
    • Ahlers, M.1    Blankenburg, R.2    Grainger, D.W.3    Meller, P.4    Ringsdorf, H.5    Salesse, C.6
  • 3
    • 0028130122 scopus 로고
    • Interfacial adsorption and aggregation associated changes in secondary structure of human calcitonin monitored by ATR-FTIR spectroscopy
    • Bauer, H. H., M. Müller, 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-FTIR spectroscopy. Biochemistry. 33:12,276-12,282.
    • (1994) Biochemistry , vol.33 , pp. 12276-12282
    • Bauer, H.H.1    Müller, M.2    Goette, J.3    Merkle, H.P.4    Fringeli, U.P.5
  • 4
    • 0018882953 scopus 로고
    • The use of avidin-biotin technology as a tool in molecular biology
    • Bayer, E. A., and M. Wilchek. 1980. The use of avidin-biotin technology as a tool in molecular biology. Methods Biochem. Anal. 26:1-46.
    • (1980) Methods Biochem. Anal. , vol.26 , pp. 1-46
    • Bayer, E.A.1    Wilchek, M.2
  • 5
    • 0018779565 scopus 로고
    • On the mode of liposome-cell interactions. Biotin conjugated lipids as ultrastructural probes
    • Bayer, E. A., B. Rivnay, and E. Skutelsky. 1979. On the mode of liposome-cell interactions. Biotin conjugated lipids as ultrastructural probes. Biochim. Biaphys. Acta. 550:464-473.
    • (1979) Biochim. Biaphys. Acta. , vol.550 , pp. 464-473
    • Bayer, E.A.1    Rivnay, B.2    Skutelsky, E.3
  • 6
    • 0001508252 scopus 로고
    • Interdependence of carbon-nitrogen and carbon-oxygen bond lengths in urea structures and in ureido ring structures
    • Blessing, R. H. 1983. Interdependence of carbon-nitrogen and carbon-oxygen bond lengths in urea structures and in ureido ring structures. J. Am. Chem. Soc. 105:2776-2783.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 2776-2783
    • Blessing, R.H.1
  • 7
    • 0022691315 scopus 로고
    • Examination of secondary structure of proteins by deconvoluted FTIR spectra
    • Byler, D. M., and H. Susi. 1986. Examination of secondary structure of proteins by deconvoluted FTIR spectra. Biopolymers. 25:469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 8
    • 0015217073 scopus 로고
    • Egg white avidin. III. Sequence of 78-residue middle cyanogen bromide peptide. Complete amino acid sequence of the protein subunit
    • DeLange, R. J., and T.-S. Huang. 1971. Egg white avidin. III. Sequence of 78-residue middle cyanogen bromide peptide. Complete amino acid sequence of the protein subunit. J. Biol. Chem. 246:698-709.
    • (1971) J. Biol. Chem. , vol.246 , pp. 698-709
    • Delange, R.J.1    Huang, T.-S.2
  • 9
    • 0015939437 scopus 로고
    • Increase in the stability of avidin produced by binding of biotin. A differential scanning calorimetric study of denaturation by heat
    • Donovan, J. W., and K. D. Ross. 1973. Increase in the stability of avidin produced by binding of biotin. A differential scanning calorimetric study of denaturation by heat. Biochemistry. 12:512-517.
    • (1973) Biochemistry , vol.12 , pp. 512-517
    • Donovan, J.W.1    Ross, K.D.2
  • 10
    • 0021196348 scopus 로고
    • The occurrence and production of avidin: A new conception of the high affinity biotin-binding protein
    • Elo, H. A., and J. Korpela. 1984. The occurrence and production of avidin: a new conception of the high affinity biotin-binding protein. Comp. Biochem. Physiol. 78B:15-20.
    • (1984) Comp. Biochem. Physiol. , vol.78 B , pp. 15-20
    • Elo, H.A.1    Korpela, J.2
  • 12
    • 0027145627 scopus 로고
    • Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: An FTIR study
    • Heimburg, T., and D. Marsh. 1993. Investigation of secondary and tertiary structural changes of cytochrome c in complexes with anionic lipids using amide hydrogen exchange measurements: an FTIR study. Biophys. J. 65:2408-2417.
    • (1993) Biophys. J. , vol.65 , pp. 2408-2417
    • Heimburg, T.1    Marsh, D.2
  • 13
    • 0026012387 scopus 로고
    • 31P NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer
    • 31P NMR spectroscopy. Correlation between the conformational changes of the protein and the lipid bilayer. Biochemistry. 30:9084-9089.
    • (1991) Biochemistry , vol.30 , pp. 9084-9089
    • Heimburg, T.1    Hildebrandt, P.2    Marsh, D.3
  • 14
    • 0020489572 scopus 로고
    • Raman spectroscopy of avidin: Secondary structure, disulphide conformation and the environment of tyrosine
    • Honzatko, R. B., and R. W. Williams. 1982. Raman spectroscopy of avidin: secondary structure, disulphide conformation and the environment of tyrosine. Biochemistry. 21:6201-6205.
    • (1982) Biochemistry , vol.21 , pp. 6201-6205
    • Honzatko, R.B.1    Williams, R.W.2
  • 15
    • 0000337013 scopus 로고
    • Fourier self-deconvolution: A method for resolving intrinsically overlapped bands
    • Kauppinen, J. K., D. J. Moffatt. H. H. Manisch, and D. G. Cameron. 1981. Fourier self-deconvolution: a method for resolving intrinsically overlapped bands. Appl. Spectrosc. 35:271-276.
    • (1981) Appl. Spectrosc. , vol.35 , pp. 271-276
    • Kauppinen, J.K.1    Moffatt, D.J.2    Manisch, H.H.3    Cameron, D.G.4
  • 16
    • 44949280032 scopus 로고
    • Two dimensional crystals of proteins on lipid layers
    • Kornberg, R. D., and S. A. Darst. 1991. Two dimensional crystals of proteins on lipid layers. Curr. Opin. Struct. Biol. 1:642-646.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 642-646
    • Kornberg, R.D.1    Darst, S.A.2
  • 17
    • 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
  • 18
    • 0024452759 scopus 로고
    • Shielding of tryptophan residues of avidin by the binding of biotin
    • Kurzban, G. P., G. Gitlin, E. A. Bayer, M. Wilchek, and P. M. Horowitz. 1989. Shielding of tryptophan residues of avidin by the binding of biotin. Biochemistry. 28:8537-8542.
    • (1989) Biochemistry , vol.28 , pp. 8537-8542
    • Kurzban, G.P.1    Gitlin, G.2    Bayer, E.A.3    Wilchek, M.4    Horowitz, P.M.5
  • 19
    • 0027164314 scopus 로고
    • Three-dimensional structures of avidin and the avidin-biotin complex
    • Livnah, O., E. A. Bayer, M. Wilchek, and J. L. Sussman. 1991 Three-dimensional structures of avidin and the avidin-biotin complex. Proc. Natl. Acad. Sci. USA. 90:5076-5080.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5076-5080
    • Livnah, O.1    Bayer, E.A.2    Wilchek, M.3    Sussman, J.L.4
  • 20
    • 0023189951 scopus 로고
    • A non-covalent method of attaching antibodies to liposomes
    • Loughrey, H., M. B. Bally, and P. Cullis. 1987. A non-covalent method of attaching antibodies to liposomes. Biochim. Biophys. Acta. 901: 157-160.
    • (1987) Biochim. Biophys. Acta. , vol.901 , pp. 157-160
    • Loughrey, H.1    Bally, M.B.2    Cullis, P.3
  • 21
    • 0025350848 scopus 로고
    • Structural studies with the uropathogenic peptide M derived from retinal s antigen
    • Muga, A., W. K. Surewicz, P. T. T. Wong, H. H. Mantsch, V. K. Singh, and R. Shinohara. 1990. Structural studies with the uropathogenic peptide M derived from retinal s antigen. Biochemistry. 29:2925-2930.
    • (1990) Biochemistry , vol.29 , pp. 2925-2930
    • Muga, A.1    Surewicz, W.K.2    Wong, P.T.T.3    Mantsch, H.H.4    Singh, V.K.5    Shinohara, R.6
  • 22
    • 0025841667 scopus 로고
    • Membrane binding induces destabilization of cytochrome c structure
    • Muga, A., H. H. Mantsch, and W. K. Surewicz. 1991. Membrane binding induces destabilization of cytochrome c structure. Biochemistry. 30: 7219-7224.
    • (1991) Biochemistry , vol.30 , pp. 7219-7224
    • Muga, A.1    Mantsch, H.H.2    Surewicz, W.K.3
  • 23
    • 0027214259 scopus 로고
    • Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 Å resolution
    • Pugliese, L., A. Coda, M. Malcovati, and M. Bolognesi. 1993. Three-dimensional structure of the tetragonal crystal form of egg-white avidin in its functional complex with biotin at 2.7 Å resolution. J. Mol. Biol. 231:698-710.
    • (1993) J. Mol. Biol. , vol.231 , pp. 698-710
    • Pugliese, L.1    Coda, A.2    Malcovati, M.3    Bolognesi, M.4
  • 24
    • 0023611168 scopus 로고
    • Use of avidin-biotin technology for liposome targeting
    • Rivnay, B., E. A. Bayer, and M. Wilchek. 1987. Use of avidin-biotin technology for liposome targeting. Methods Enzymol. 149:119-123.
    • (1987) Methods Enzymol. , vol.149 , pp. 119-123
    • Rivnay, B.1    Bayer, E.A.2    Wilchek, M.3
  • 25
    • 0025007841 scopus 로고
    • Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy
    • Surewicz, W. K., J. J. Leddy, and H. H. Mantsch. 1990. Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy. Biochemistry. 29:8106-8111.
    • (1990) Biochemistry , vol.29 , pp. 8106-8111
    • Surewicz, W.K.1    Leddy, J.J.2    Mantsch, H.H.3
  • 26
    • 0027221844 scopus 로고
    • Interaction of avidin with spin-labeled N-biotinyl phosphatidylethanolamine
    • Swamy, M. J., and D. Marsh. 1993. Interaction of avidin with spin-labeled N-biotinyl phosphatidylethanolamine. FEBS Lett. 324:56-58.
    • (1993) FEBS Lett. , vol.324 , pp. 56-58
    • Swamy, M.J.1    Marsh, D.2
  • 27
    • 0028135686 scopus 로고
    • Spin-label electron spin resonance studies on the dynamics of different phases of N-biotinyl-phosphatidylethanolamines
    • Swamy, M. J., and D. Marsh. 1994. Spin-label electron spin resonance studies on the dynamics of different phases of N-biotinyl-phosphatidylethanolamines. Biochemistry. 33:11,656-11,663.
    • (1994) Biochemistry , vol.33 , pp. 11656-11663
    • Swamy, M.J.1    Marsh, D.2
  • 28
    • 0027382338 scopus 로고
    • 31P-NMR studies of N-biotinyl phosphalidylethanolamines
    • 31P-NMR studies of N-biotinyl phosphalidylethanolamines. Biochemistry. 32:9960-9967.
    • (1993) Biochemistry , vol.32 , pp. 9960-9967
    • Swamy, M.J.1    Würz, U.2    Marsh, D.3
  • 29
    • 0028069688 scopus 로고
    • Differential scanning calorimetry of thermotropic phase transitions in vitaminylated lipids: Aqueous dispersions of N-biotinyl phosphatidylethanolamines
    • Swamy, M. J., B. Angerstein, and D. Marsh. 1994. Differential scanning calorimetry of thermotropic phase transitions in vitaminylated lipids: aqueous dispersions of N-biotinyl phosphatidylethanolamines. Biophys. J. 66:31-39.
    • (1994) Biophys. J. , vol.66 , pp. 31-39
    • Swamy, M.J.1    Angerstein, B.2    Marsh, D.3
  • 30
    • 0019159353 scopus 로고
    • Tumor-associated ganglio-N-triosylceramide. Target for antibody-dependent, avidin-mediated drug killing of tumor cells
    • Urdal, D. L., and S. Hakomori. 1980. Tumor-associated ganglio-N-triosylceramide. Target for antibody-dependent, avidin-mediated drug killing of tumor cells. J. Biol. Chem. 255:10,509-10,516.
    • (1980) J. Biol. Chem. , vol.255 , pp. 10509-10516
    • Urdal, D.L.1    Hakomori, S.2
  • 31
    • 0024588901 scopus 로고
    • Structural origins of high-affinity biotin binding to streptavidin
    • Weber, P. C., D. H. Ohlendorf, J. J. Wendeloski, and F. R. Salemme. 1989. Structural origins of high-affinity biotin binding to streptavidin. Science. 243:85-88.
    • (1989) Science , vol.243 , pp. 85-88
    • Weber, P.C.1    Ohlendorf, D.H.2    Wendeloski, J.J.3    Salemme, F.R.4
  • 32
    • 0026606240 scopus 로고
    • Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin
    • Weber, P. C., J. J. Wendeloski, M. W. Pantoliano, and F. R. Salemme. 1992. Crystallographic and thermodynamic comparison of natural and synthetic ligands bound to streptavidin. J. Am. Chem. Soc. 114: 3197-3200.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3197-3200
    • Weber, P.C.1    Wendeloski, J.J.2    Pantoliano, M.W.3    Salemme, F.R.4
  • 33
    • 0024741801 scopus 로고
    • Avidin-biotin technology ten years on: Has it lived lip to its expectations?
    • Wilchek, M., and E. A. Bayer. 1989. Avidin-biotin technology ten years on: Has it lived lip to its expectations? Trends Biochem. Sci. 14: 408-412.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 408-412
    • Wilchek, M.1    Bayer, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.