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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Richards, John H. Gray, Harry B. Winkler, Jay R. Kim, Judy E. Arjara, Gitrada |
| Description | Author Affiliation: Kim JE ( Beckman Institute and Department of Chemistry, California Institute of Technology, Pasadena, California 91125, USA.) |
| Abstract | Steady-state and time-resolved fluorescence measurements on each of five native tryptophan residues in full-length and truncated variants of E. coli outer-membrane protein A (OmpA) have been made in folded and denatured states. Tryptophan singlet excited-state lifetimes are multiexponential and vary among the residues. In addition, substantial increases in excited-state lifetimes accompany OmpA folding, with longer lifetimes in micelles than in phospholipid bilayers. This finding suggests that the Trp environments of OmpA folded in micelles and phospholipid bilayers are different. Measurements of Trp fluorescence decay kinetics with full-length OmpA folded in brominated lipid vesicles reveal that W102 is the most distant fluorophore from the hydrocarbon core, while W7 is the closest. Steady-state and time-resolved polarized fluorescence measurements indicate reduced Trp mobility when OmpA is folded in a micelle, and even lower mobility when the protein is folded in a bilayer. The fluorescence properties of truncated OmpA, in which the soluble periplasmic domain is removed, only modestly differ from those of the full-length form, suggesting similar folded structures for the two forms under these conditions. |
| ISSN | 15206106 |
| e-ISSN | 15205207 |
| Journal | The Journal of Physical Chemistry B |
| Issue Number | 35 |
| Volume Number | 110 |
| Language | English |
| Publisher | American Chemical Society (United States) |
| Publisher Date | 2006-09-07 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Bacterial Outer Membrane Proteins Chemistry Biophysics Tryptophan Anisotropy Circular Dichroism Dimyristoylphosphatidylcholine Escherichia Coli Metabolism Kinetics Micelles Molecular Conformation Mutation Protein Folding Protein Structure, Tertiary Spectrometry, Fluorescence Urea Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Physical chemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Surfaces, Coatings and Films Materials Chemistry Medicine Physical and Theoretical Chemistry |
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