메뉴 건너뛰기




Volumn 76, Issue 2-3, 1998, Pages 267-275

Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate

Author keywords

15N filtered NOESY; Amphipathic helix; Chemical shift index; Lecithin:cholesterol acyltransferase

Indexed keywords

APOLIPOPROTEIN; DODECYL SULFATE SODIUM; LOW DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; VERY LOW DENSITY LIPOPROTEIN; APOLIPOPROTEIN C; APOLIPOPROTEIN C1;

EID: 0032247180     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o98-053     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A., and Davis, D.G. 1985. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65: 355-360.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-360
    • Bax, A.1    Davis, D.G.2
  • 2
    • 0000195671 scopus 로고
    • Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy
    • Bodenhausen, G., and Ruben, D.J. 1980. Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem. Phys. Lett. 69: 185-189.
    • (1980) Chem. Phys. Lett. , vol.69 , pp. 185-189
    • Bodenhausen, G.1    Ruben, D.J.2
  • 3
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani, D.W., Rogers, D.P., Engler, J.A., and Brouillette, C.G. 1997. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. U.S.A. 94: 12 291-12 296.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 4
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L., and Ernst, R.R. 1983. Coherence transfer by isotropic mixing: application to proton correlation spectroscopy. J. Magn. Reson. 53: 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 6
    • 0030060665 scopus 로고    scopus 로고
    • Structural studies of a peptide activator of human lecithin-cholesterol acyltransferase
    • Buchko, G.W., Treleaven, W.D., Dunne, S.J., Tracey, A.S., and Cushley, R.J. 1996. Structural studies of a peptide activator of human lecithin-cholesterol acyltransferase. J. Biol. Chem. 271: 3039-3045.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3039-3045
    • Buchko, G.W.1    Treleaven, W.D.2    Dunne, S.J.3    Tracey, A.S.4    Cushley, R.J.5
  • 7
    • 0015512255 scopus 로고
    • Tangier disease. Report of a case and studies of lipid metabolism
    • Clifton-Bligh, P., Nestel, P.J., and Whyte, H.M. 1972. Tangier disease. Report of a case and studies of lipid metabolism. N. Engl. J. Med. 286: 567-571.
    • (1972) N. Engl. J. Med. , vol.286 , pp. 567-571
    • Clifton-Bligh, P.1    Nestel, P.J.2    Whyte, H.M.3
  • 9
    • 0000859818 scopus 로고
    • Application of isotope-filtered 2D NOE experiments in the conformational analysis of atrial natriuretic factor(7-23)
    • Fesik, S.W., Gampe, R.T., and Rockway, T.W. 1987. Application of isotope-filtered 2D NOE experiments in the conformational analysis of atrial natriuretic factor(7-23). J. Magn. Reson. 74: 366-371.
    • (1987) J. Magn. Reson. , vol.74 , pp. 366-371
    • Fesik, S.W.1    Gampe, R.T.2    Rockway, T.W.3
  • 10
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B.H., Bachmann, P., and Ernst, R.R. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71: 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 12
    • 0017401503 scopus 로고
    • Repeated helical pattern in apolipoprotein-A-I
    • McLachlan, A.D. 1977. Repeated helical pattern in apolipoprotein-A-I. Nature (London), 267: 465-466.
    • (1977) Nature (London) , vol.267 , pp. 465-466
    • McLachlan, A.D.1
  • 15
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto, M., Saudek, V., and Sklenar, V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR, 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 17
    • 49549146155 scopus 로고
    • Quadrature Fourier NMR detection: Simple multiplex for dual detection and discussion
    • Redfield, A.G., and Kunz, S.D. 1975. Quadrature Fourier NMR detection: simple multiplex for dual detection and discussion. J. Magn. Reson. 19: 250-254.
    • (1975) J. Magn. Reson. , vol.19 , pp. 250-254
    • Redfield, A.G.1    Kunz, S.D.2
  • 18
    • 0029019322 scopus 로고
    • Conformation of two peptides corresponding to human apolipoprotein C-I residues 7-24 and 35-53 in the presence of sodium dodecyl sulfate by CD and NMR spectroscopy
    • Rozek, A., Buchko, G.W., and Cushley, R.J. 1995. Conformation of two peptides corresponding to human apolipoprotein C-I 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
  • 20
    • 0000988302 scopus 로고
    • Edited by P.C. Jost & O.H. Griffith, John Wiley and Sons, New York
    • Scanu, A.M., Edelstein, C., and Shen, B.W. 1982. In Lipid-protein interactions. Vol.1. Edited by P.C. Jost & O.H. Griffith, John Wiley and Sons, New York. pp. 259-316.
    • (1982) Lipid-protein Interactions , vol.1 , pp. 259-316
    • Scanu, A.M.1    Edelstein, C.2    Shen, B.W.3
  • 22
    • 0015950692 scopus 로고
    • A molecular theory of lipid-protein interactions in the plasma lipoproteins
    • Segrest, J.P., Jackson, R.L., Morrisett, J.D., and Gotto, A.M., Jr. 1974. A molecular theory of lipid-protein interactions in the plasma lipoproteins. FEBS Lett. 38: 247-258.
    • (1974) FEBS Lett. , vol.38 , pp. 247-258
    • Segrest, J.P.1    Jackson, R.L.2    Morrisett, J.D.3    Gotto A.M., Jr.4
  • 25
    • 0016409177 scopus 로고
    • The complete amino acid sequence of C-I (apoLp-Ser), an apolipoprotein from human very low density lipoproteins
    • Shulman, R.S., Herbert, P.N., Wehrly, K., and Fredrickson, D.S. 1975. The complete amino acid sequence of C-I (apoLp-Ser), an apolipoprotein from human very low density lipoproteins. J. Biol. Chem. 250: 182-190.
    • (1975) J. Biol. Chem. , vol.250 , pp. 182-190
    • Shulman, R.S.1    Herbert, P.N.2    Wehrly, K.3    Fredrickson, D.S.4
  • 26
    • 0017135639 scopus 로고
    • The solid phase synthesis of a protein activator for lecithin:cholesterol acyltransferase corresponding to human plasma apoC-I
    • Sigler, G.F., Soutar, A.K., Smith, L.C., Gotto, A.M., Jr., and Sparrow, J.T. 1976. The solid phase synthesis of a protein activator for lecithin:cholesterol acyltransferase corresponding to human plasma apoC-I. Proc. Nat.l Acad. Sci. U.S.A. 73: 1422-1426.
    • (1976) Proc. Nat.l Acad. Sci. U.S.A. , vol.73 , pp. 1422-1426
    • Sigler, G.F.1    Soutar, A.K.2    Smith, L.C.3    Gotto A.M., Jr.4    Sparrow, J.T.5
  • 28
    • 0016814761 scopus 로고
    • Effect of the human plasma apolipoproteins and phosphatidylcholine acyl donor on the activity of lecithin:cholesterol acyltransferase
    • Soutar, A.K., Garner, C.W., Baker, H.N., Sparrow, J.T., Jackson, R.L., Gotto, A.M., and Smith, L.C. 1975. Effect of the human plasma apolipoproteins and phosphatidylcholine acyl donor on the activity of lecithin:cholesterol acyltransferase. Biochemistry, 14: 3057-3064.
    • (1975) Biochemistry , vol.14 , pp. 3057-3064
    • Soutar, A.K.1    Garner, C.W.2    Baker, H.N.3    Sparrow, J.T.4    Jackson, R.L.5    Gotto, A.M.6    Smith, L.C.7
  • 29
    • 0018254107 scopus 로고
    • Lecithin:cholesterol acyltransferase activation and lipid binding by synthetic fragments of apolipoprotein C-I
    • Soutar, A.K., Sigler, G.F., Smith, L.C., Gotto, A.M., Jr., and Sparrow, J.T. 1978. Lecithin:cholesterol acyltransferase activation and lipid binding by synthetic fragments of apolipoprotein C-I. Scand. J. Clin. Lab. Invest. Suppl. 150: 53-58.
    • (1978) Scand. J. Clin. Lab. Invest. Suppl. , vol.150 , pp. 53-58
    • Soutar, A.K.1    Sigler, G.F.2    Smith, L.C.3    Gotto A.M., Jr.4    Sparrow, J.T.5
  • 30
    • 0030237213 scopus 로고    scopus 로고
    • Improvements to the TMSBr method of peptide resin deprotection and cleavage: Application to large peptides
    • Sparrow, J.T., and Monera, O.D. 1996. Improvements to the TMSBr method of peptide resin deprotection and cleavage: application to large peptides. Pept. Res. 9: 218-222.
    • (1996) Pept. Res. , vol.9 , pp. 218-222
    • Sparrow, J.T.1    Monera, O.D.2
  • 31
    • 0028010952 scopus 로고
    • Effect of apolipoprotein C-I peptides on the apolipoprotein E content and receptor-binding properties of beta-migrating very low density lipoproteins
    • Swaney, J.B., and Weisgraber, K.H. 1994. Effect of apolipoprotein C-I peptides on the apolipoprotein E content and receptor-binding properties of beta-migrating very low density lipoproteins. J. Lipid Res. 35: 134-142.
    • (1994) J. Lipid Res. , vol.35 , pp. 134-142
    • Swaney, J.B.1    Weisgraber, K.H.2
  • 33
    • 0030875963 scopus 로고    scopus 로고
    • Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional heteronuclear NMR techniques
    • Wang, J., Gagne, S.M., Sykes, B.D., and Ryan, R.O. 1997a. Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional heteronuclear NMR techniques. J. Biol. Chem. 272: 17 912-17 920.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17912-17920
    • Wang, J.1    Gagne, S.M.2    Sykes, B.D.3    Ryan, R.O.4
  • 34
    • 0030815233 scopus 로고    scopus 로고
    • The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy
    • Wang, G., Sparrow. J.T., and Cushley, R.J. 1997b. The helix-hinge-helix structural motif in human apolipoprotein A-I determined by NMR spectroscopy. Biochemistry, 36: 13 657-13 666.
    • (1997) Biochemistry , vol.36 , pp. 13657-13666
    • Wang, G.1    Sparrow, J.T.2    Cushley, R.J.3
  • 35
    • 0025611153 scopus 로고
    • Apolipoprotein C-I modulates the interaction of apolipoprotein E with beta-migrating very low density lipoproteins (beta-VLDL) and inhibits binding of beta-VLDL to low density lipoprotein receptor-related protein
    • Weisgraber, K.H., Mahley, R.W., Kowal, R.C., Herz, J., Goldstein, J.L., and Brown, M.S. 1990. Apolipoprotein C-I modulates the interaction of apolipoprotein E with beta-migrating very low density lipoproteins (beta-VLDL) and inhibits binding of beta-VLDL to low density lipoprotein receptor-related protein. J. Biol. Chem. 265: 22 453-22 459.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22453-22459
    • Weisgraber, K.H.1    Mahley, R.W.2    Kowal, R.C.3    Herz, J.4    Goldstein, J.L.5    Brown, M.S.6
  • 36
  • 37
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart, D.S., and Sykes, B.D. 1994. Chemical shifts as a tool for structure determination. Methods Enzymol. 239: 363-392.
    • (1994) Methods Enzymol. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 38
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D.S., Sykes, B.D., and Richards, F.M. 1991. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222: 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 39
    • 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., and 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
  • 40
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR, 5: 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.