PMID:10899627
| Citation |
Greene, MK, Steede, NK and Landry, SJ (2000) Domain-specific spectroscopy of 5-hydroxytryptophan-containing variants of Escherichia coli DnaJ. Biochim. Biophys. Acta 1480:267-77 |
|---|---|
| Abstract |
Tryptophan-containing variants of Escherichia coli DnaJ protein were constructed in order to examine the hypothetical domain structure by fluorescence quenching and denaturant-induced unfolding. Two residues in the J-domain and one in the Gly/Phe-rich region were targeted for replacement and the proteins were expressed in a tryptophan auxotrophic strain in the presence of 5-hydroxytryptophan (5-HW). Fluorescence quenching with iodide of 5-HW in the variant proteins suggests that the Gly/Phe-rich region is more accessible to solvent than the J-domain. This is consistent with the proposal that the Gly/Phe-rich region is unstructured. Unfolding of the 5-HW-containing variants was monitored by fluorescence, and the results showed that the unfolding of the J-domain is cooperative and the unfolding of the Gly/Phe-rich region is not cooperative. |
| Links | |
| Keywords |
5-Hydroxytryptophan/chemistry; Circular Dichroism; Escherichia coli/chemistry; Escherichia coli Proteins; HSP40 Heat-Shock Proteins; Heat-Shock Proteins/chemistry; Models, Molecular; Protein Denaturation; Recombinant Proteins/chemistry; Spectrometry, Fluorescence; Thermodynamics |
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