Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1968 May;60(1):108–114. doi: 10.1073/pnas.60.1.108

Triplet-triplet energy transfer in proteins as a criterion of proximity.

W C Galley, L Stryer
PMCID: PMC539087  PMID: 4968632

Full text

PDF
108

Selected References

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

  1. Chen R. F., Kernohan J. C. Combination of bovine carbonic anhydrase with a fluorescent sulfonamide. J Biol Chem. 1967 Dec 25;242(24):5813–5823. [PubMed] [Google Scholar]
  2. ERLANGER B. F., COOPER A. G., BENDICH A. J. ON THE HETEROGENEITY OF THREE-TIMES-CRYSTALLIZED ALPHA-CHYMOTRYPSIN. Biochemistry. 1964 Dec;3:1880–1883. doi: 10.1021/bi00900a015. [DOI] [PubMed] [Google Scholar]
  3. Fridborg K., Kannan K. K., Liljas A., Lundin J., Strandberg B., Strandberg R., Tilander B., Wirén G. Crystal structure of human erythrocyte carbonic anhydrase C. 3. Molecular structure of the enzyme and of one enzyme-inhibitor complex at 5-5 A resolution. J Mol Biol. 1967 May 14;25(3):505–516. doi: 10.1016/0022-2836(67)90202-1. [DOI] [PubMed] [Google Scholar]
  4. Hartley B. S., Kauffman D. L. Corrections to the amino acid sequence of bovine chymotrypsinogen A. Biochem J. 1966 Oct;101(1):229–231. doi: 10.1042/bj1010229. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. LINDSKOG S., NYMAN P. O. METAL-BINDING PROPERTIES OF HUMAN ERYTHROCYTE CARBONIC ANHYDRASES. Biochim Biophys Acta. 1964 Jun 1;85:462–474. doi: 10.1016/0926-6569(64)90310-4. [DOI] [PubMed] [Google Scholar]
  6. LINDSKOG S. Purification and properties of bovine erythrocyte carbonic anhydrase. Biochim Biophys Acta. 1960 Apr 8;39:218–226. doi: 10.1016/0006-3002(60)90156-6. [DOI] [PubMed] [Google Scholar]
  7. MARSHALL F. J., SIGAL M. V., Jr, SULLIVAN H. R., CESNIK C., ROOT M. A. FURTHER STUDIES ON N-ARYLSULFONYL-N-ALKYLUREAS. J Med Chem. 1963 Jan;6:60–63. doi: 10.1021/jm00337a014. [DOI] [PubMed] [Google Scholar]
  8. Maren T. H. Carbonic anhydrase: chemistry, physiology, and inhibition. Physiol Rev. 1967 Oct;47(4):595–781. doi: 10.1152/physrev.1967.47.4.595. [DOI] [PubMed] [Google Scholar]
  9. Matthews B. W., Sigler P. B., Henderson R., Blow D. M. Three-dimensional structure of tosyl-alpha-chymotrypsin. Nature. 1967 May 13;214(5089):652–656. doi: 10.1038/214652a0. [DOI] [PubMed] [Google Scholar]
  10. Pocker Y., Stone J. T. The catalytic versatility of erythrocyte carbonic anhydrase. 3. Kinetic studies of the enzyme-catalyzed hydrolysis of p-nitrophenyl acetate. Biochemistry. 1967 Mar;6(3):668–678. doi: 10.1021/bi00855a005. [DOI] [PubMed] [Google Scholar]
  11. Stryer L., Haugland R. P. Energy transfer: a spectroscopic ruler. Proc Natl Acad Sci U S A. 1967 Aug;58(2):719–726. doi: 10.1073/pnas.58.2.719. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Truong T., Bersohn R., Brumer P., Luk C. K., Tao T. Effect of pH on the phosphorescence of tryptophan, tyrosine, and proteins. J Biol Chem. 1967 Jun 25;242(12):2979–2985. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES