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Volumn 132, Issue 18, 2010, Pages 6324-6328

Structural variations in the cross-β core of amyloid β fibrils revealed by deep uv resonance raman spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; COMMON STRUCTURES; DEEP UV; FIBRILLOGENESIS; GLOBULAR PROTEINS; HYDROGEN-DEUTERIUM EXCHANGE; MOLECULAR LEVELS; PEPTIDE CONFORMATION; POST MORTEM; QUANTITATIVE CHARACTERIZATION; SOLID STATE NMR; STRUCTURAL CHARACTERIZATION; STRUCTURAL DATA; STRUCTURAL VARIATIONS;

EID: 77952075172     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja909074j     Document Type: Article
Times cited : (62)

References (37)
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Dobson, C. M. Nature 2003, 426, 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 11
    • 77952079462 scopus 로고    scopus 로고
    • We use the term "conformation" as a set of dihedral angles of peptide backbone, in accordance with the definition of Tycko-s group
    • We use the term "conformation" as a set of dihedral angles of peptide backbone, in accordance with the definition of Tycko-s group.
  • 30
    • 0009861670 scopus 로고    scopus 로고
    • Bandwidth
    • Chalmers, J. M. and Griffiths, P. R., Eds.; Wiley: Chichester, U.K.
    • Turner, J. J. Bandwidth. In Handbook of Vibrational Spectroscopy; Chalmers, J. M. and Griffiths, P. R., Eds.; Wiley: Chichester, U.K., 2001; Vol. 1, pp 101 - 127.
    • (2001) Handbook of Vibrational Spectroscopy , vol.1 , pp. 101-127
    • Turner, J.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.