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Volumn 39, Issue 1, 2006, Pages 6-8

Native structure and degradation pattern of silk sericin studied by 13C NMR spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

ELECTROPHORESIS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; PYROLYSIS; SPINNING (FIBERS); STRUCTURAL ANALYSIS;

EID: 30944438539     PISSN: 00249297     EISSN: None     Source Type: Journal    
DOI: 10.1021/ma0521147     Document Type: Article
Times cited : (43)

References (29)
  • 15
    • 0345956573 scopus 로고    scopus 로고
    • National Institute of Agrobiological Sciences: Tsukuba, Japan
    • Yamamoto, T.; Miyajima, T.; Mase, K.; Iizuka, T. In Annual Report 2002; National Institute of Agrobiological Sciences: Tsukuba, Japan, 2002; pp 24-25.
    • (2002) Annual Report , vol.2002 , pp. 24-25
    • Yamamoto, T.1    Miyajima, T.2    Mase, K.3    Iizuka, T.4
  • 23
    • 30944461463 scopus 로고    scopus 로고
    • note
    • 13C NMR spectrum of the regenerated sericin solution (Figure 3a) exhibited much smaller peaks assignable to Glu, Phe, and Tyr residues than native sericin solution (Figure la), showing that low molecular weight impurities can be removed during regeneration process. The Cα and Cβ chemical shifts of major amino acids in the regenerated sericin solution were in good agreement with those of native sericin solution, which demonstrated that sericin remained in a largely random coil structure after regeneration from the cocoon.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.