Skip to main content
Biophysical Journal logoLink to Biophysical Journal
. 1995 Mar;68(3):1191–1195. doi: 10.1016/S0006-3495(95)80295-X

Approaches to teaching fluorescence spectroscopy.

C A Royer 1
PMCID: PMC1281842  PMID: 7756538

Full text

PDF
1191

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amir D., Haas E. Reduced bovine pancreatic trypsin inhibitor has a compact structure. Biochemistry. 1988 Dec 13;27(25):8889–8893. doi: 10.1021/bi00425a003. [DOI] [PubMed] [Google Scholar]
  2. Beechem J. M., Brand L. Time-resolved fluorescence of proteins. Annu Rev Biochem. 1985;54:43–71. doi: 10.1146/annurev.bi.54.070185.000355. [DOI] [PubMed] [Google Scholar]
  3. Eftink M. R. The use of fluorescence methods to monitor unfolding transitions in proteins. Biophys J. 1994 Feb;66(2 Pt 1):482–501. doi: 10.1016/s0006-3495(94)80799-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Grinvald A., Steinberg I. Z. The fluorescence decay of tryptophan residues in native and denatured proteins. Biochim Biophys Acta. 1976 Apr 14;427(2):663–678. doi: 10.1016/0005-2795(76)90210-5. [DOI] [PubMed] [Google Scholar]
  5. Harris D. L., Hudson B. S. Photophysics of tryptophan in bacteriophage T4 lysozymes. Biochemistry. 1990 Jun 5;29(22):5276–5285. doi: 10.1021/bi00474a009. [DOI] [PubMed] [Google Scholar]
  6. Heyduk T., Lee J. C. Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction. Proc Natl Acad Sci U S A. 1990 Mar;87(5):1744–1748. doi: 10.1073/pnas.87.5.1744. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. James E., Wu P. G., Stites W., Brand L. Compact denatured state of a staphylococcal nuclease mutant by guanidinium as determined by resonance energy transfer. Biochemistry. 1992 Oct 27;31(42):10217–10225. doi: 10.1021/bi00157a008. [DOI] [PubMed] [Google Scholar]
  8. Kim S. J., Chowdhury F. N., Stryjewski W., Younathan E. S., Russo P. S., Barkley M. D. Time-resolved fluorescence of the single tryptophan of Bacillus stearothermophilus phosphofructokinase. Biophys J. 1993 Jul;65(1):215–226. doi: 10.1016/S0006-3495(93)81070-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lakowicz J. R., Weber G. Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry. 1973 Oct 9;12(21):4171–4179. doi: 10.1021/bi00745a021. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LeTilly V., Royer C. A. Fluorescence anisotropy assays implicate protein-protein interactions in regulating trp repressor DNA binding. Biochemistry. 1993 Aug 3;32(30):7753–7758. doi: 10.1021/bi00081a021. [DOI] [PubMed] [Google Scholar]
  11. Neyroz P., Brand L., Roseman S. Sugar transport by the bacterial phosphotransferase system. The intrinsic fluorescence of enzyme I. J Biol Chem. 1987 Nov 25;262(33):15900–15907. [PubMed] [Google Scholar]
  12. Ross J. B., Schmidt C. J., Brand L. Time-resolved fluorescence of the two tryptophans in horse liver alcohol dehydrogenase. Biochemistry. 1981 Jul 21;20(15):4369–4377. doi: 10.1021/bi00518a021. [DOI] [PubMed] [Google Scholar]
  13. Silva J. L., Weber G. Pressure stability of proteins. Annu Rev Phys Chem. 1993;44:89–113. doi: 10.1146/annurev.pc.44.100193.000513. [DOI] [PubMed] [Google Scholar]
  14. Tuschl T., Gohlke C., Jovin T. M., Westhof E., Eckstein F. A three-dimensional model for the hammerhead ribozyme based on fluorescence measurements. Science. 1994 Nov 4;266(5186):785–789. doi: 10.1126/science.7973630. [DOI] [PubMed] [Google Scholar]
  15. Weber G., Farris F. J. Synthesis and spectral properties of a hydrophobic fluorescent probe: 6-propionyl-2-(dimethylamino)naphthalene. Biochemistry. 1979 Jul 10;18(14):3075–3078. doi: 10.1021/bi00581a025. [DOI] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES