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Volumn 105, Issue 44, 2001, Pages 10992-10999

Ultrafast structural relaxation of myoglobin following photodissociation of carbon monoxide probed by time-resolved resonance Raman spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

MYOGLOBIN;

EID: 0035829917     PISSN: 10895647     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp010923w     Document Type: Article
Times cited : (67)

References (57)
  • 6
    • 0002052550 scopus 로고
    • The heme protein structure and the iron histidine stretching mode
    • Spiro, T.G., Ed.; John Wiley & Sons: New York
    • Kitagawa, T. The Heme Protein Structure and the Iron Histidine Stretching Mode. In Biological Applications of Raman Spectroscopy; Spiro, T.G., Ed.; John Wiley & Sons: New York, 1987; Vol. III, p 97.
    • (1987) Biological Applications of Raman Spectroscopy , vol.3 , pp. 97
    • Kitagawa, T.1
  • 7
    • 0001257259 scopus 로고
    • Transient and cryogenic studies of photodissociated hemoglobin and myoglobin
    • Spiro, T.G., Ed.; John Wiley & Sons: New York
    • Rousseau, D.L.; Friedman, J.M. Transient and Cryogenic Studies of Photodissociated Hemoglobin and Myoglobin. In Biological Applications of Raman Spectroscopy; Spiro, T.G., Ed.; John Wiley & Sons: New York, 1987; Vol. III, p 133.
    • (1987) Biological Applications of Raman Spectroscopy , vol.3 , pp. 133
    • Rousseau, D.L.1    Friedman, J.M.2
  • 31
    • 0011380425 scopus 로고    scopus 로고
    • note
    • 9 band to temporal changes of the zeroth and first moments observed in the present study is supposed to be negligible.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.