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Volumn 306, Issue 1, 2001, Pages 69-79

The solution structure of C1-T1, a two-domain proteinase inhibitor derived from a circular precursor protein from Nicotiana alata

Author keywords

Domain interactions; Nicotiana alata; Nuclear magnetic resonance spectroscopy; Protein structure; Proteinase inhibitors

Indexed keywords

AMINO ACID; PROTEIN PRECURSOR; PROTEINASE INHIBITOR;

EID: 0035830486     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4318     Document Type: Article
Times cited : (17)

References (44)
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    • Determination of three-dimensional structures of proteins by simulated annealing with interproton distance constraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2
    • (1988) Protein Eng. , vol.2 , pp. 27-38
    • Nilges, M.1    Gronenborn, A.M.2    Brünger, A.T.3    Clore, G.M.4
  • 42
    • 0024815191 scopus 로고
    • Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing
    • (1989) J. Mol. Biol. , vol.210 , pp. 635-648
    • Holak, T.A.1    Gondol, D.2    Otlewski, J.3    Wilusz, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.