Dynamics of compact denatured states of glutaminyl-tRNA synthetase probed by bis-ANS binding kinetics
- 18 October 2000
- journal article
- Published by Elsevier in Biophysical Chemistry
- Vol. 87 (2-3) , 201-212
- https://doi.org/10.1016/s0301-4622(00)00192-7
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Aging of Tubulin Monomers Using 5,5'-Bis(8-anilino-1-naphthalenesulfonate) as a ProbeBiochemistry, 1995
- Compact Intermediates States in Protein FoldingPublished by Springer Nature ,1995
- Protein Conformational Changes Induced by 1,1'-Bis(4-anilino-5-naphthalenesulfonic acid): Preferential Binding to the Molten Globule of DnaKBiochemistry, 1994
- Unfolded proteins, compact states and molten globulesCurrent Opinion in Structural Biology, 1992
- A fluorescence spectroscopic study of glutaminyl‐tRNA synthetase from Escherichia coli and its implications for the enzyme mechanismEuropean Journal of Biochemistry, 1991
- DENATURED STATES OF PROTEINSAnnual Review of Biochemistry, 1991
- Protein folding: Hypotheses and experimentsProtein Journal, 1987
- Bis(8-anilinonaphthalene-1-sulfonate) as a probe for tubulin decayBiochemistry, 1986
- Preparation, crystalline structure, and spectral properties of the fluorescent probe 4,4'-bis-1-phenylamino-8-naphthalenesulfonateJournal of the American Chemical Society, 1978
- Size Distribution of Polypeptide Chains in CellsNature, 1970