This title appears in the Scientific Report :
2009
Please use the identifier:
http://dx.doi.org/10.1002/cbic.200800739 in citations.
Observing Proteins as Single Molecules Encapsulated in Surface-Tethered Polymeric Nanocontainers
Observing Proteins as Single Molecules Encapsulated in Surface-Tethered Polymeric Nanocontainers
Immobilizing biomolecules provides the advantage of observing them individually for extended time periods, which is impossible to accomplish for freely diffusing molecules in solution. In order to immobilize individual protein molecules, we encapsulated them in polymeric vesicles made of amphiphilic...
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Personal Name(s): | Rosenkranz, T. |
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Katranidis, A. / Atta, D. / Enderlein, J. / Gregor, I. / Grzelakowski, M. / Rigler, P. / Meier, W. / Fitter, J. | |
Contributing Institute: |
Molekulare Biophysik; ISB-2 |
Published in: | ChemBioChem, 10 (2009) S. 702 - 709 |
Imprint: |
Weinheim
Wiley-VCH
2009
|
Physical Description: |
702 - 709 |
PubMed ID: |
19191249 |
DOI: |
10.1002/cbic.200800739 |
Document Type: |
Journal Article |
Research Program: |
Programm Biosoft |
Series Title: |
ChemBioChem
10 |
Subject (ZB): | |
Publikationsportal JuSER |
Immobilizing biomolecules provides the advantage of observing them individually for extended time periods, which is impossible to accomplish for freely diffusing molecules in solution. In order to immobilize individual protein molecules, we encapsulated them in polymeric vesicles made of amphiphilic triblock copolymers and tethered the vesicles to a cover slide surface. A major goal of this study is to investigate polymeric vesicles with respect to their suitability for protein-folding studies. The fact that polymeric vesicles possess an extreme stability under various chemical conditions is supported by our observation that harsh unfolding conditions do not perturb the structural integrity of the vesicles. Moreover, polymerosomes prove to be permeable to GdnHCl and, thereby, ideally suited for unfolding and refolding studies with encapsulated proteins. We demonstrate this with encapsulated phosphoglycerate kinase, which was fluorescently labeled with Atto655, a dye that exhibits pronounced photoinduced electron transfer (PET) to a nearby tryptophan residue in the native state. Under unfolding conditions, PET was reduced, and we monitored alternating unfolding and refolding conditions for individual encapsulated proteins. |