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Volumn 100, Issue 29, 1996, Pages 12034-12042

Evidence for damped hemoglobin dynamics in a room temperature trehalose glass

Author keywords

[No Author keywords available]

Indexed keywords

DISSOCIATION; FLUORESCENCE; GLASS; KINETIC THEORY; MOLECULAR DYNAMICS; PHYSICAL CHEMISTRY;

EID: 0030198111     PISSN: 00223654     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp9609489     Document Type: Article
Times cited : (115)

References (72)
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    • Ross, J. B. A.; Eftink, M. R. In Time-Resolved Laser Spectroscopy in Biochemistry III; Lakowicz, J. R., Ed.; The Society of Photo-optical Instrumentation Engineers: Bellingham, WA, 1992; pp 2-9.
    • (1992) Time-Resolved Laser Spectroscopy in Biochemistry III , pp. 2-9
    • Ross, J.B.A.1    Eftink, M.R.2
  • 9
    • 0025929570 scopus 로고
    • Methods of Biochemical Analysis, Suelter, C. H., Ed.; John Wiley & Sons: New York
    • Eftink, M. R. In Methods of Biochemical Analysis, Vol. 35: Protein Structure Determination; Suelter, C. H., Ed.; John Wiley & Sons: New York, 1991; pp 127-205.
    • (1991) Vol. 35: Protein Structure Determination , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 15
    • 0028290597 scopus 로고
    • Everse, J., Vandegriff, K. D., Winslow, R. M., Eds.; Academic Press: San Diego, CA
    • Hirsch, R. E. In Hemoglobins, Part C, Biophysical Methods: Methods in Enzymology; Everse, J., Vandegriff, K. D., Winslow, R. M., Eds.; Academic Press: San Diego, CA, 1994; Vol. 232, pp 231-246.
    • (1994) Hemoglobins, Part C, Biophysical Methods: Methods in Enzymology , vol.232 , pp. 231-246
    • Hirsch, R.E.1
  • 31
    • 33748403635 scopus 로고
    • Lakowicz, J. R., Ed.; The Society of Photo-optical Instrumentation Engineers: Bellingham, WA
    • Holtom, G. In Time-Resolved Laser Spectroscopy in Biochemistry II; Lakowicz, J. R., Ed.; The Society of Photo-optical Instrumentation Engineers: Bellingham, WA, 1990; pp 433-464.
    • (1990) Time-Resolved Laser Spectroscopy in Biochemistry II , pp. 433-464
    • Holtom, G.1
  • 34
    • 77957095245 scopus 로고
    • Hirs, C. H. W., Timasheff, S. N., Eds.; Academic Press: Orlando, FL, Chapter 16
    • Johnson, M. L.; Frasier, S. G. In Enzyme Structure, Part J; Methods in Enzymology; Hirs, C. H. W., Timasheff, S. N., Eds.; Academic Press: Orlando, FL, 1985; Vol. 117, Chapter 16, pp 301-342.
    • (1985) Enzyme Structure, Part J; Methods in Enzymology , vol.117 , pp. 301-342
    • Johnson, M.L.1    Frasier, S.G.2
  • 39
    • 0028308524 scopus 로고
    • Everse, J.; Vandegriff, K. D., Winslow, R. M., Eds.; Academic Press: San Diego, CA
    • Friedman, J. M in Hemoglobins, Part C, Biophysical Methods: Methods in Enzymology; Everse, J.; Vandegriff, K. D., Winslow, R. M., Eds.; Academic Press: San Diego, CA, 1994; Vol. 232, pp 205-231.
    • (1994) Hemoglobins, Part C, Biophysical Methods: Methods in Enzymology , vol.232 , pp. 205-231
    • Friedman, J.M.1
  • 42
    • 85033038778 scopus 로고    scopus 로고
    • note
    • i is only true if the emission spectra for the different fluorescing populations is the same. Given the large bandwidth of the tryptophan emission spectrum, small shifts in emission maximum will have only minor effects.
  • 45
    • 85033072400 scopus 로고    scopus 로고
    • Manuscript in preparation
    • Levin, L.; Friedman, J. Manuscript in preparation.
    • Levin, L.1    Friedman, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.