| Autor: |
Greene MK; Department of Biochemistry (SL43), Tulane University School of Medicine, 1430 Tulane Avenue, New Orleans, LA 70112-2699, USA., Steede NK, Landry SJ |
| Jazyk: |
angličtina |
| Zdroj: |
Biochimica et biophysica acta [Biochim Biophys Acta] 2000 Jul 14; Vol. 1480 (1-2), pp. 267-77. |
| DOI: |
10.1016/s0167-4838(00)00078-9 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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