• Publications
  • Influence
Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis.
Comparison of the present results with other studies on the molten globule formed at acid pH in the lipocalin family suggests that above 65 degrees C a partly unfolded state is formed, possibly by destabilization of the intermolecular beta-strand I and the loss of the main helix, but it is not a classical molten globules transition.
Iron in the basal ganglia in Parkinson's disease. An in vitro study using extended X-ray absorption fine structure and cryo-electron microscopy.
Investigation of the physical environment of brain iron in post-mortem tissue showed that iron levels are increased in two areas of the brain in Parkinson's disease including the substantia nigra, the site of maximal neurodegeneration, which produces increased loading of ferritin, which is the normal brain iron storage protein.
The alpha-helix folds on the millisecond time scale.
It is shown here that helix nucleation, in fact, takes place on the millisecond time scale, and that the transient overshoot of helix content significantly greater than at equilibrium is caused by the formation of a single long helix followed by its breakage into the two or more helices present at equilibrium.
CD12: a new high-flux beamline for ultraviolet and vacuum-ultraviolet circular dichroism on the SRS, Daresbury.
The commissioning and characterization of an SRS bending-magnet beamline constructed for the measurement of vacuum-ultraviolet circular dichroism on biological and other materials is described and the impact that the new beamline is likely to have is speculated on.
Single-molecule imaging and fluorescence lifetime imaging microscopy show different structures for high- and low-affinity epidermal growth factor receptors in A431 cells.
The results of single-molecule Förster resonant energy transfer analysis in combination with ensemble fluorescence lifetime imaging microscopy support a structural model in which asymmetric EGFR head-to-head interfaces may be relevant for HA EGFR oligomerization.
Circular Dichroism in Protein Folding Studies
  • D. Clarke
  • Chemistry, Medicine
    Current protocols in protein science
  • 1 November 2012
This unit describes the procedures for performing CD experiments for the study of protein folding, and identifies commonly encountered problems and their solutions.
Hydrophobic Fluorescent Probes Introduce Artifacts into Single Molecule Tracking Experiments Due to Non-Specific Binding
This systematic investigation of how different dye chemistries influence the behaviour of spectrally similar fluorescent probes indicates that dye chemistry has a strong influence on the propensity of dye-protein conjugates to adhere non-specifically to the substrate.
Light flux density threshold at which protein denaturation is induced by synchrotron radiation circular dichroism beamlines.
The estimation of a flux density threshold under which SRCD beamlines should be operated when samples are to be exposed to low-wavelength vacuum ultraviolet radiation for extended periods of time is led to.
Human Epidermal Growth Factor Receptor (EGFR) Aligned on the Plasma Membrane Adopts Key Features of Drosophila EGFR Asymmetry
It is found that the asymmetry of this structure shares key features with that of the Drosophila EGFR, suggesting that the structural basis for negative cooperativity is conserved from invertebrates to humans but that in human EGFR the extracellular region asymmetry requires interactions with the plasma membrane.