메뉴 건너뛰기




Volumn 118, Issue 19, 1996, Pages 4654-4664

An interpretive basis of the proton nuclear magnetic resonance hyperfine shifts for structure determination of high-spin ferric hemoproteins. Implications for the reversible thermal unfolding of ferricytochrome c′ from Rhodopseudomonas palustris

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C; HEMOPROTEIN;

EID: 0029942913     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja953719t     Document Type: Article
Times cited : (33)

References (29)
  • 2
    • 0001023705 scopus 로고
    • Ciayton, R. K., Sistrom, W. R., Eds.: Plenum Press: New York, NY.
    • Bartsch, R. G. The Photosynthetic Bacteria; Ciayton, R. K., Sistrom, W. R., Eds.: Plenum Press: New York, NY. 1978; pp 249-279.
    • (1978) The Photosynthetic Bacteria , pp. 249-279
    • Bartsch, R.G.1
  • 17
    • 5144233105 scopus 로고
    • Bax, A.; Davis, D. G. J. Magn. Reson. 1985, 65, 355-260. Cavanagh, J.; Ranee, M. J. Magn. Reson. 1990, 88, 72-85.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355-1260
    • Bax, A.1    Davis, D.G.2
  • 18
    • 44949289665 scopus 로고
    • Bax, A.; Davis, D. G. J. Magn. Reson. 1985, 65, 355-260. Cavanagh, J.; Ranee, M. J. Magn. Reson. 1990, 88, 72-85.
    • (1990) J. Magn. Reson. , vol.88 , pp. 72-85
    • Cavanagh, J.1    Ranee, M.2
  • 19
    • 0000690113 scopus 로고
    • ls for the four heme methyls are the same in spite of their significant differences in contact shift dictates that the relaxation of the heme methyl is insignificantly influenced by delocalized spin density and hence is dominated by dipolar relaxation by the spin density of the iron (Unger, S. W.; Jue, T.; La Mar, G. N. J. Magn. Reson. 1985, 61, 448-456).
    • (1985) J. Magn. Reson. , vol.61 , pp. 448-456
    • Unger, S.W.1    Jue, T.2    La Mar, G.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.