Fluorescent Probes for Conformational States of Proteins. I. Mechanism of Fluorescence of 2-p-Toluidinylnaphthalene-6-sulfonate, a Hydrophobic Probe*
- 1 June 1966
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 5 (6) , 1908-1919
- https://doi.org/10.1021/bi00870a018
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- FRAGMENTATION OF BOVINE SERUM ALBUMIN BY PEPSIN .1. ORIGIN OF ACID EXPANSION OF ALBUMIN MOLECULE1964
- The effect of temperature on the fluorescence of some aromatic amino acids and proteinsBiochimica et Biophysica Acta, 1962
- PHYSICAL STUDIES OF LYSOZYME .1. CHARACTERIZATION1962
- Physical and Chemical Studies of a Limited Reaction of Iodine with ProteinsJournal of Biological Chemistry, 1959
- Observations on the electrophoretic and ultracentrifugal changes accompanying the activation of chymotrypsinogenArchives of Biochemistry and Biophysics, 1955
- IDENTIFICATION OF A PEPTIDE RELEASED DURING AUTOCATALYTIC ACTIVATION OF TRYPSINOGENJournal of Biological Chemistry, 1955
- Polarization of the fluorescence of macromolecules. 1. Theory and experimental methodBiochemical Journal, 1952
- A study of the adsorption of dyes on bovine serum albumin by the method of polarization of fluorescenceBiochemical Journal, 1952
- Polarization of the fluorescence of macromolecules. 2. Fluorescent conjugates of ovalbumin and bovine serum albuminBiochemical Journal, 1952
- THE MOLECULAR SIZE AND SHAPE OF THE PANCREATIC PROTEASES .3. ALPHA-CHYMOTRYPSIN1951