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Volumn 71, Issue 6, 1996, Pages 3442-3447

13C NMR of Nephila clavipes major ampullate silk gland

Author keywords

[No Author keywords available]

Indexed keywords

FIBROIN; GLUCOSE; PROLINE; ALANINE; CARBON; INSECT PROTEIN;

EID: 0030346864     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(96)79539-5     Document Type: Article
Times cited : (223)

References (32)
  • 1
    • 0000951118 scopus 로고
    • 13C cross polarization-magic angle spinning NMR, X-ray diffraction, and infrared spectroxcopy
    • 13C cross polarization-magic angle spinning NMR, X-ray diffraction, and infrared spectroxcopy. Macromolecules. 18:1841-1845.
    • (1985) Macromolecules , vol.18 , pp. 1841-1845
    • Asakura, T.1    Kuzuhara, A.2    Tabeta, R.3    Saito, H.4
  • 2
    • 0001124562 scopus 로고
    • 13C NMR study of the chain dynamics and solution structure of Bombyx mori silk fibroin
    • 13C NMR study of the chain dynamics and solution structure of Bombyx mori silk fibroin. Macromolecules. 17:1075-1081.
    • (1984) Macromolecules , vol.17 , pp. 1075-1081
    • Asakura, T.1    Watanabe, Y.2    Uchida, A.3    Minagawa, H.4
  • 3
    • 0014547285 scopus 로고
    • Changes in fine structure during silk protein production in the ampullate gland of the spider Arenus sericatus
    • Bell, A. L., amd D. B. Peakall. 1969. Changes in fine structure during silk protein production in the ampullate gland of the spider Arenus sericatus. J. Cell Biol. 42:284-295.
    • (1969) J. Cell Biol. , vol.42 , pp. 284-295
    • Bell, A.L.1    Peakall, D.B.2
  • 4
    • 0019005874 scopus 로고
    • Determination of protein secondary structure in solution by vacuum ultroviolet circular dichroism
    • Brahms, S., and J. Brahms. 1980. Determination of protein secondary structure in solution by vacuum ultroviolet circular dichroism. J. Mol. Biol. 138:149-178.
    • (1980) J. Mol. Biol. , vol.138 , pp. 149-178
    • Brahms, S.1    Brahms, J.2
  • 5
    • 0023710642 scopus 로고
    • The "molten globule" state is involved in the transolcation of proteins across membranes?
    • Bychkova, V. E., R. H. Pain, and O. B. Ptitsyn. 1988. The "molten globule" state is involved in the transolcation of proteins across membranes? FEBS Lett. 238:231-234.
    • (1988) FEBS Lett. , vol.238 , pp. 231-234
    • Bychkova, V.E.1    Pain, R.H.2    Ptitsyn, O.B.3
  • 6
    • 84986492408 scopus 로고
    • A spider fibroin and its synthesis
    • Candelas, G., and J. Cintron. 1981. A spider fibroin and its synthesis. J. Exp. Zool. 216:1-6.
    • (1981) J. Exp. Zool. , vol.216 , pp. 1-6
    • Candelas, G.1    Cintron, J.2
  • 7
    • 0028061986 scopus 로고
    • Equilibrium unfolding of Escherichia coli ribonuclease H: Characterization of a partially folded state
    • Dabora, J. M., and S. Marqusee. 1994. Equilibrium unfolding of Escherichia coli ribonuclease H: characterization of a partially folded state. Protein Sci. 3:1401-1408.
    • (1994) Protein Sci. , vol.3 , pp. 1401-1408
    • Dabora, J.M.1    Marqusee, S.2
  • 8
    • 0028188303 scopus 로고
    • Chemical shifts of carbonyl carbons in peptides and proteins
    • de Dios, A. C., and E. Oldfield. 1994. Chemical shifts of carbonyl carbons in peptides and proteins. J. Am. Chem. Soc. 116:11485-11488.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11485-11488
    • De Dios, A.C.1    Oldfield, E.2
  • 11
    • 0026731378 scopus 로고
    • Does Fourier-transform infrared spectroscopy provide useful information on protein structures?
    • Haris, P. I., and D. Chapman. 1992. Does Fourier-transform infrared spectroscopy provide useful information on protein structures? Trends Biochem. Sci. 17:328-333.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 328-333
    • Haris, P.I.1    Chapman, D.2
  • 12
    • 0026657815 scopus 로고
    • Isolation of a clone encoding a second dragline silk fibroin
    • Hinman, M. B., and R. V. Lewis. 1992. Isolation of a clone encoding a second dragline silk fibroin. J. Biol. Chem. 267:19320-19324.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19320-19324
    • Hinman, M.B.1    Lewis, R.V.2
  • 14
    • 0009715073 scopus 로고
    • The physico-chemical properties of silk fibers and the fiber spinning process
    • Iizuka, E. 1983. The physico-chemical properties of silk fibers and the fiber spinning process. Experientia. 39:499-454.
    • (1983) Experientia , vol.39 , pp. 499-1454
    • Iizuka, E.1
  • 15
    • 0001294092 scopus 로고
    • Molecular weight distribution of Nephila clavipes dragline silk
    • Jackson, C., and J. O'Brien. 1995. Molecular weight distribution of Nephila clavipes dragline silk. Macromolecules. 28:5975-5977.
    • (1995) Macromolecules , vol.28 , pp. 5975-5977
    • Jackson, C.1    O'Brien, J.2
  • 17
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins Struct. Funct. Genet. 6:87-103.
    • (1989) Proteins Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 19
    • 11944263043 scopus 로고
    • Spider silk, the unraveling of a mystery
    • Lewis, R. V. 1992. Spider silk, the unraveling of a mystery. Acc. Chem. Res. 25:392-398.
    • (1992) Acc. Chem. Res. , vol.25 , pp. 392-398
    • Lewis, R.V.1
  • 20
    • 85030290325 scopus 로고
    • Spider silk: Nature's high performance fiber
    • Presented at the 207th National Meeting of the American Chemical Society, San Diego, CA, March 13-17, 1994
    • Mello, C. M., K. Senecal, B. Yeung, P. Vouros, and D. L. Kaplan. 1994. Spider silk: nature's high performance fiber. Presented at the 207th National Meeting of the American Chemical Society, San Diego, CA, March 13-17, 1994. Abstr. Papers Am. Chem. Soc. 207:67-79.
    • (1994) Abstr. Papers Am. Chem. Soc. , vol.207 , pp. 67-79
    • Mello, C.M.1    Senecal, K.2    Yeung, B.3    Vouros, P.4    Kaplan, D.L.5
  • 25
    • 28544433674 scopus 로고
    • 13C NMR of Nephila clavipes dragline silk establishes structure and identity of crystalline regions
    • 13C NMR of Nephila clavipes dragline silk establishes structure and identity of crystalline regions. Macromolecules. 27:5235-5237.
    • (1994) Macromolecules , vol.27 , pp. 5235-5237
    • Simmons, A.1    Ray, E.2    Jelinski, L.W.3
  • 26
    • 0347610773 scopus 로고
    • Empirical correlation between protein backbone conformation and C-alpha and C-beta carbon-13 NMR chemical shifts
    • Spera, S., and A. Bax. 1991. Empirical correlation between protein backbone conformation and C-alpha and C-beta carbon-13 NMR chemical shifts. J. Am. Chem. Soc. 113:5490-5492.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 27
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susie, H., and D. M. Byler. 1986. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 130:290-311.
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susie, H.1    Byler, D.M.2
  • 29
    • 0001113739 scopus 로고
    • Water extraction by the major ampullate duct during silk formation in the spider Arigiope aurantia lucas
    • Tillinghast, E. K., F. S. Chase, and M. A. Townley. 1984. Water extraction by the major ampullate duct during silk formation in the spider Arigiope aurantia lucas. J. Insect Physiol. 30:591-596.
    • (1984) J. Insect Physiol. , vol.30 , pp. 591-596
    • Tillinghast, E.K.1    Chase, F.S.2    Townley, M.A.3
  • 31
    • 0002392785 scopus 로고
    • An apparatus and technique for the forcible silking of spiders
    • Work, R. W., and P. D. Emerson. 1982. An apparatus and technique for the forcible silking of spiders. J. Arachnol. 10:1-10.
    • (1982) J. Arachnol. , vol.10 , pp. 1-10
    • Work, R.W.1    Emerson, P.D.2
  • 32
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., C. S. C. Wu, and H. M. Martinez. 1986. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.C.2    Martinez, H.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.