Intramolecular Excitonic Dimers in Protease Substrates: Modification of the Backbone Moiety To Probe the H-Dimer Structure
- 14 February 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 102 (10) , 1820-1827
- https://doi.org/10.1021/jp973419t
Abstract
No abstract availableKeywords
This publication has 8 references indexed in Scilit:
- Characterization of fluorescence quenching in bifluorophoric protease substratesBiophysical Chemistry, 1997
- Structural Characteristics of Fluorophores That Form Intramolecular H-Type Dimers in a Protease SubstrateThe Journal of Physical Chemistry B, 1997
- Profluorescent protease substrates: intramolecular dimers described by the exciton model.Proceedings of the National Academy of Sciences, 1996
- Tetramethylrhodamine Dimer Formation as a Spectroscopic Probe of the Conformation of Escherichia coli Ribosomal Protein L7/L12 DimersPublished by Elsevier ,1996
- Energy Transfer, Charge Transfer, and Proton Transfer in Molecular Composite SystemsPublished by Springer Nature ,1991
- Optimization by Simulated AnnealingScience, 1983
- Fluorescent tetramethyl rhodamine derivatives of α-bungarotoxin: Preparation, separation, and characterizationAnalytical Biochemistry, 1977
- Energy Transfer Mechanisms and the Molecular Exciton Model for Molecular AggregatesRadiation Research, 1963