Prof Sonia Antoranz Contera: Publications

Dynamics of bacteriorhodopsin 2D crystal observed by high-speed atomic force microscopy.

J Struct Biol 167:2 (2009) 153-158

Authors:

Hayato Yamashita, Kislon Voïtchovsky, Takayuki Uchihashi, Sonia Antoranz Contera, John F Ryan, Toshio Ando

Abstract:

We have used high-speed atomic force microscopy to study the dynamics of bacteriorhodopsin (bR) molecules at the free interface of the crystalline phase that occurs naturally in purple membrane. Our results reveal temporal fluctuations at the crystal edges arising from the association and dissociation of bR molecules, most predominantly pre-formed trimers. Analysis of the dissociation kinetics yields an estimate of the inter-trimer single-bond energy of -0.9kcal/mol. Rotational motion of individual bound trimers indicates that the inter-trimer bond involves W10-W12 tryptophan residues.

DNA Conformation and Biomolecular Motors: New Nanomedicine Research Targets

Biophysical Journal Elsevier 96:3 (2009) 345a

Authors:

Sonia Trigueros, Sonia Contera, John Ryan

High Resolution AFM of KcsA Structure and Clustering in a Lipid Bilayer

Biophysical Journal Elsevier 96:3 (2009) 370a

Authors:

Joanna A Sobek, Sonia Antoranz Contera, Sonia Trigueros, Constantina Fotinou, Frances M Ashcroft, JF Ryan

Nanotubes As Drug Delivery Systems For Prokaryotic And Eukaryotic Cells

Biophysical Journal Elsevier 96:3 (2009) 51a

Authors:

Sonia Antoranz Contera, Sonia Trigueros, JF Ryan

Doping of carbon nanotubes with nitrogen improves protein coverage whilst retaining correct conformation.

Nanotechnology 19:38 (2008) 384001

Authors:

Hilary J Burch, Sonia Antoranz Contera, Maurits RR de Planque, Nicole Grobert, JF Ryan

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.

51��