STRUCTURAL OBSERVATION OF A SINGLE, RECONSTITUTED IONOTROPIC GLUTAMATE RECEPTOR IN LIPID BILAYER
JOURNAL OF PHYSIOLOGICAL SCIENCES 59 (2009) 394-394
Elastic modulus of suspended purple membrane measured by atomic force microscopy
Applied Surface Science 254:23 (2008) 7877-7880
Abstract:
We have probed the mechanical properties of purple membrane (PM) in a physiological environment using the atomic force microscope (AFM). By suspending PM over nano-trenches, the elastic properties of PM can be evaluated free from the interaction with the substrate. Force-displacement curves were obtained on the suspended membrane and the data was compared to that of a simple model of a thin film over a trench. By fitting the data to the model, the elastic modulus of PM was estimated to be 8 MPa. When the membrane is repeatedly indented, we observed a change in the force-distance data consistent with damage to the two-dimensional crystal of PM. In this paper we demonstrate that the AFM allows us to evaluate the mechanics of biological membranes in their native conditions. © 2008 Elsevier B.V. All rights reserved.Doping of carbon nanotubes with nitrogen improves protein coverage whilst retaining correct conformation.
Nanotechnology 19:38 (2008) 384001
Abstract:
Relevant parameters for non-covalent protein functionalization of carbon nanotubes are explored. Multiwalled carbon nanotubes are carboxylated and functionalized with metalloproteins. Using atomic force microscopy (AFM) we quantitatively determine that coverage with nitrogen-doped multiwalled carbon nanotubes is superior compared to coverage with un-doped multiwalled carbon nanotubes, due to enhanced carboxylation. Conformational analysis using a combination of AFM, antibody binding assays, circular dichroism and UV-visible spectroscopy demonstrates that the metalloproteins retain their native structure when adsorbed to nitrogen-doped multiwalled carbon nanotubes irrespective of their size, charge or folding motif.Inter-oligomer interactions of the human prion protein are modulated by the polymorphism at codon 129.
J Mol Biol 381:1 (2008) 212-220
Abstract:
The common polymorphism at codon 129 in the human prion protein (PrP) has been shown in many studies to influence not only the pathology of prion disease but also the misfolding propensity of PrP. Here we used NMR, CD and atomic force microscopy in solution to investigate differences in beta-oligomer (beta(O)) formation and inter-oligomer interaction depending on the polymorphism at codon 129. NMR investigations assigned the observable amide resonances to the beta(O) N-terminal segments, showing that it is the core region of PrP (residues 127-228) that is involved in beta(O) formation. Atomic force microscopy revealed distinctive 1.8 x 15 x 15-nm disk-like structures that form stacks through inter-oligomer interactions. The propensity to form stacks and the number of oligomers involved depended on the polymorphism at codon 129, with a significantly lower degree of stacking for beta(O) with valine at position 129. This result provides evidence for conformational differences between the beta(O) allelic forms, showing that the core region of the protein including position 129 is actively involved in inter-oligomer interactions, consistent with NMR observations.Effect of acid treatment on the structure and electrical properties of nitrogen-doped multiwalled carbon nanotubes
Journal of Physical Chemistry C 112:6 (2008) 1908-1912