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Zeitschrift für Physikalische Chemie

International journal of research in physical chemistry and chemical physics

Ed. by Rademann, Klaus

12 Issues per year

IMPACT FACTOR 2016: 1.012

CiteScore 2016: 0.99

SCImago Journal Rank (SJR) 2016: 0.463
Source Normalized Impact per Paper (SNIP) 2016: 0.470

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Volume 221, Issue 1 (Jan 2007)


Ultrasensitive Fluorescence Microscopy Studies of Protein Interactions with Functionalized Surfaces

Colin D. Heyes / G. Ulrich Nienhaus
Published Online: 2008-05-27 | DOI: https://doi.org/10.1524/zpch.2007.221.1.75

Controlling protein adsorption to surfaces is an important issue in biotechnology, biomedicine and basic sciences. Proteins readily adsorb non-specifically to a variety of surfaces in a process known as biofouling, which is a major problem in the biomedical, environmental and industrial fields that can be solved by pre-treating the surfaces with adsorption-resistant materials. Additionally, surfaces can be structured and functionalized so as to immobilize proteins in specific patterns, orientations and/or densities, which is important in such areas as biosensors, biocatalysis, biotechnology, protein microarrays and single molecule biophysics. Here we review the various surface modifications and bioconjugation techniques that have been used in these areas. We also introduce novel fluorescence microscopy techniques, which have been employed to analyze the resistance of the surfaces to non-specific adsorption with detection limits down to the single molecule. A huge advantageous property of fluorescence microscopy is its sensitivity to the structure of individual, immobilized proteins by using Förster resonance energy transfer (FRET). Thus one can examine if the surface coating maintains the folded, functional form of specifically immobilized proteins. We then describe several important advances in studying slow timescale biophysical processes such as protein folding of single, specifically immobilized proteins. Future directions into which this field is expected to progress are also discussed.

Keywords: Single Molecule Fluorescence; RNase H; Patterning; Biofouling; Protein Folding

About the article

Received: 2006-04-20

Accepted: 2006-07-27

Published Online: 2008-05-27

Published in Print: 2007-01-01

Citation Information: Zeitschrift für Physikalische Chemie, ISSN (Online) 2196-7156, ISSN (Print) 0942-9352, DOI: https://doi.org/10.1524/zpch.2007.221.1.75.

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