Biofunctionalized Polymer Surfaces Exhibiting Minimal Interaction towards Immobilized Proteins
2004; Wiley; Volume: 5; Issue: 4 Linguagem: Inglês
10.1002/cphc.200400024
ISSN1439-7641
AutoresElza V. Amirgoulova, Jürgen Gröll, Colin D. Heyes, Thomas Ameringer, Carlheinz Röcker, Martin Möller, G. Ulrich Nienhaus,
Tópico(s)Biotin and Related Studies
ResumoAn 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.
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