New approaches, rooted in the physical sciences, have been developed to gain a more fundamental understanding of protein–GAG (glycosaminoglycan) interactions. DPI (dual polarization interferometry) is an optical technique, which measures real-time changes in the mass of molecules bound at a surface and the geometry of the bound molecules. QCM-D (quartz crystal microbalance-dissipation), an acoustic technique, measures the mass and the viscoelastic properties of adsorbates. The FTIR (Fourier-transform IR) amide bands I, II and III, resulting from the peptide bond, provide insight into protein secondary structure. Synchrotron radiation CD goes to much shorter wavelengths than laboratory CD, allowing access to chromophores that provide insights into the conformation of the GAG chain and of β-strand structures of proteins. To tackle the diversity of GAG structure, we are developing noble metal nanoparticle probes, which can be detected at the level of single particles and so enable single molecule biochemistry and analytical chemistry. These new approaches are enabling new insights into structure–function relationships in GAGs and together they will resolve many of the outstanding problems in this field.
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Conference Article|
May 22 2006
Protein–GAG interactions: new surface-based techniques, spectroscopies and nanotechnology probes
E.A. Yates;
E.A. Yates
*Centre for Nanoscale Science, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, U.K.
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C.J. Terry;
C.J. Terry
*Centre for Nanoscale Science, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, U.K.
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C. Rees;
C. Rees
*Centre for Nanoscale Science, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, U.K.
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T.R. Rudd;
T.R. Rudd
*Centre for Nanoscale Science, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, U.K.
†Centre for Nanoscale Science, Department of Chemistry, University of Liverpool, Liverpool L69 7ZB, U.K.
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L. Duchesne;
L. Duchesne
*Centre for Nanoscale Science, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, U.K.
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M.A. Skidmore;
M.A. Skidmore
*Centre for Nanoscale Science, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, U.K.
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R. Lévy;
R. Lévy
*Centre for Nanoscale Science, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, U.K.
†Centre for Nanoscale Science, Department of Chemistry, University of Liverpool, Liverpool L69 7ZB, U.K.
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N.T.K. Thanh;
N.T.K. Thanh
*Centre for Nanoscale Science, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, U.K.
†Centre for Nanoscale Science, Department of Chemistry, University of Liverpool, Liverpool L69 7ZB, U.K.
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R.J. Nichols;
R.J. Nichols
†Centre for Nanoscale Science, Department of Chemistry, University of Liverpool, Liverpool L69 7ZB, U.K.
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D.T. Clarke;
D.T. Clarke
‡CCLRC, Daresbury Laboratory, Warrington, Cheshire WA4 4AD, U.K.
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D.G. Fernig
D.G. Fernig
1
*Centre for Nanoscale Science, School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, U.K.
1To whom correspondence should be addressed, at School of Biological Sciences, Biosciences Building, Crown Street, University of Liverpool, Liverpool L69 7ZB, U.K. (email dgfernig@liv.ac.uk).
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Publisher: Portland Press Ltd
Received:
December 20 2005
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2006 The Biochemical Society
2006
Biochem Soc Trans (2006) 34 (3): 427–430.
Article history
Received:
December 20 2005
Citation
E.A. Yates, C.J. Terry, C. Rees, T.R. Rudd, L. Duchesne, M.A. Skidmore, R. Lévy, N.T.K. Thanh, R.J. Nichols, D.T. Clarke, D.G. Fernig; Protein–GAG interactions: new surface-based techniques, spectroscopies and nanotechnology probes. Biochem Soc Trans 1 June 2006; 34 (3): 427–430. doi: https://doi.org/10.1042/BST0340427
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