Disc coablation and epidural injection of steroids: a comparison of strategies in the treatment of mechanical spinal discogenic pain

Summary In this study two strategies in the treatment of Mechanical Spinal Discogenic Pain have been compared: Disc Coablation and Epidural Injection of Steroids. In 2003 50 patients treated with one or two epidural injections have been selected ''ad random'' and 50 patients treated with disc coablation. Comparison of the data indicated an improvement of average VAS when relaxed for both groups ðp < 0:01Þ, while after slightmoderate strain, this value was significant only after coablation ðp < 0:001Þ. Finally, average VAS was clearly lower ðp < 0:01Þ after coablation as compared to epidural injections

Ligation Tunes Protein Reactivity in an Ancient Haemoglobin: Kinetic Evidence for an Allosteric Mechanism in Methanosarcina acetivorans Protoglobin

Protoglobin from Methanosarcina acetivorans (MaPgb) is a dimeric globin with peculiar structural properties such as a completely buried haem and two orthogonal tunnels connecting the distal cavity to the solvent. CO binding to and dissociation from MaPgb occur through a biphasic kinetics. We show that the heterogenous kinetics arises from binding to (and dissociation from) two tertiary conformations in ligation-dependent equilibrium. Ligation favours the species with high binding rate (and low dissociation rate). The equilibrium is shifted towards the species with low binding (and high dissociation) rates for the unliganded molecules. A quantitative model is proposed to describe the observed carbonylation kinetics

Native and unfolded states of phosphoglycerate kinase studied by single molecule FRET

Single-molecule Förster resonance energy transfer (FRET) measurements with phosphoglycerate kinase from yeast were performed at different concentrations of guanidine hydrochloride. From these steady-state measurements we obtained FRET efficiency histograms characterizing structural properties of individual proteins at different stages between the native and the fully unfolded state. Native proteins exhibit a slightly more expanded structure under buffer conditions without denaturant as compared to conditions with denaturant. At 0.5 M GndHCl an unfolded state population that exhibits a significantly expanded structure as compared to the native state, emerges. The unfolded state is characterized by a pronounced broadening of the efficiency distribution, which indicates a large structural and/or dynamical heterogeneity within the population. At high denaturant concentrations, well above the unfolding transition at C(1/2)~0.7 M, we observe a progressive expansion of the protein structure, namely globule-coil transition