Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/216074

Title

Biofunctionalized polymer surfaces exhibiting minimal interaction towards immobilized proteins

Author(s)

Amirgoulova, Elza V.;  Groll, Juergen;  Heyes, Colin D.;  Ameringer, Thomas;  Roecker, Carlheinz;  Moeller, Martin;  Nienhaus, G. Ulrich

Abstract

An invisible surface: single protein molecules were immobilized on a cross-linked polymer surface (see cartoon), and imaged using fluorescence resonance energy transfer (FRET). The surface not only maintained the correct conformation of the protein molecules, but also allowed them to be unfolded and refolded fifty times consecutively. Moreover, the measured δG, cooperativity and the transition midpoint in guanidinium chloride of the unfolding-folding transition on the surface was identical to the protein in solution. Thus, the surface is energetically 'invisible' to the folding protein.

Publication type

Journal article

Source

ChemPhysChem, Vol. 5, no. 4 (Apr 2004), pp. 552-555

Publication year

2004

FOR Code(s)

0202 Atomic, Molecular, Nuclear, Particle and Plasma Physics;  0306 Physical Chemistry (Incl. Structural);  0307 Theoretical and Computational Chemistry

Keyword(s)

Binding sites;  Bioenergy;  Biosensors;  Confocal microscopy;  Cross linking;  Fluorescence resonance energy transfer;  Guanidine hydrochloride;  Molecular interaction;  Polymers;  Protein conformation;  Protein folding;  Protein interaction;  Single-molecule studies;  Surface chemistry;  Surface properties

Publisher

Wiley-VCH Verlag

ISSN

1439-4235

Publisher URL

http://dx.doi.org/10.1002/cphc.200400024

Copyright

Copyright © 2004 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Peer reviewed