Use of intrinsic fluorescence to follow the denaturation of vicilin, a storage protein from Vicia faba
- 12 January 1987
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 29 (1) , 9-20
- https://doi.org/10.1111/j.1399-3011.1987.tb02225.x
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Stability of vicilin, a legume seed storage protein, with step‐wise electrostatic modificationInternational Journal of Peptide and Protein Research, 1985
- Tyrosinate fluorescence maxima at 345 nm in proteins lacking tryptophan at pH 7FEBS Letters, 1978
- Fluorescence of proteins in aqueous neutral salt solutions. I. Influence of anionsBiopolymers, 1977
- FLUORESCENCE AND THE LOCATION OF TRYPTOPHAN RESIDUES IN PROTEIN MOLECULESPhotochemistry and Photobiology, 1973
- The structure of vicilin of Vicia fabaPhytochemistry, 1972
- THE FLUORESCENCE OF NATIVE, DENATURED AND REDUCED‐DENATURED PROTEINS*Photochemistry and Photobiology, 1971
- A COMPARISON OF SOME PROPERTIES OF VICILIN AND LEGUMIN ISOLATED FROM SEEDS OF PISUM SATIVUM, VICIA FABA AND CICER ARIETINUMNew Phytologist, 1969
- Fluorescence Quantum Yields of Tryptophan and TyrosineAnalytical Letters, 1967
- Fluorescence and protein structure IX. Relationship between tyrosine fluorescence and various stages in denaturation of ribonucleaseBiochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis, 1966
- Structural transitions of lysozyme in urea solutionBiochimica et Biophysica Acta, 1962