Peptide Sequence and Conformation Strongly Influence Tryptophan Fluorescence
Open Access
- 15 March 2008
- journal article
- Published by Elsevier in Biophysical Journal
- Vol. 94 (6) , 2280-2287
- https://doi.org/10.1529/biophysj.107.116921
Abstract
No abstract availableKeywords
Funding Information
- National Institutes of Health (GM 37039 GM33216, GM 52483)
- Welch Foundation (A1543, BE-1060, BE-1281)
This publication has 34 references indexed in Scilit:
- Tryptophan Fluorescence Reveals the Presence of Long-Range Interactions in the Denatured State of Ribonuclease SaBiophysical Journal, 2008
- Mechanism of the Highly Efficient Quenching of Tryptophan Fluorescence in Human γD-CrystallinBiochemistry, 2006
- pK values of the ionizable groups of proteinsProtein Science, 2006
- Dependence of Tryptophan Emission Wavelength on Conformation in Cyclic HexapeptidesThe Journal of Physical Chemistry B, 2006
- Quantitative Prediction of Fluorescence Quantum Yields for Tryptophan in ProteinsThe Journal of Physical Chemistry B, 2004
- Additive Transfer Free Energies of the Peptide Backbone Unit That Are Independent of the Model Compound and the Choice of Concentration ScaleBiochemistry, 2004
- Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- How to measure and predict the molar absorption coefficient of a proteinProtein Science, 1995
- Fluorescence Techniques for Studying Protein StructurePublished by Wiley ,1991
- Multifrequency Phase and Modulation FluorometryAnnual Review of Biophysics and Bioengineering, 1984