Crustal fault reactivation facilitating lithospheric folding/buckling in the central Indian Ocean

High-quality, normal-incidence seismic reflection data confirm that tectonic deformation in the central Indian Ocean occurs at two spatial scales: whole lithosphere folding with wavelengths varying between 100 and 300 km, and compressional reactivation of crustal faults with a characteristic spacing of c. 5 km. Faults penetrate through the crust and probably into the upper mantle. Both types of deformation are driven by regional large intraplate stresses originating from the Indo-Eurasian collision. Numerical modelling of the spatial and temporal relationships between these two modes of deformations shows that, in agreement with geophysical observations, crustal faults are reactivated first with stick-slip behaviour. Subsequent lithospheric folding does not start until horizontal loading has significantly reduced the mechanical strength of the lithosphere, as predicted by elasto-plastic buckling theory. Modelling suggests that lithospheric folding does not develop in the absence of fault reactivation. Crustal fault reactivation, therefore, appears to be a key facilitating mechanism for oceanic lithospheric buckling in the central Indian Ocean

Microfacies analysis and metre-scale cyclicity in the Givetian back-reef sediments of south-east

Garland, J., Tucker, M.E., and Scrutton, C. T. 1996. Microfacies analysis and metre-scale cyclicity in the Givetian back-reef sediments of south-east Devon. Proceedings of the Ussher Society, 9, 031-036 The Givetian (Middle Devonian) of south-east Devon consists of reef and back-reef facies (Tor Bay Reef-Complex) developed on a shelf-edge rise. Three sections in the Newton Abbot area have recently been studied with emphasis on detailed logging, sampling and thin section analysis of the back-reef sediments. Eight microfacies have been identified ranging from shallow subtidal to exposed supratidal deposits, forming four groups. 1. Semi-restricted subtidal -stromatoporoid floatstones, low-energy accumulations, least restricted facies -Stachyodes rudstones, high-energy back-reef talus 2. Restricted subtidal -Amphipora floatstones, low-energy accumulations -gastropod packstones, back-reef sedimentation with temporary agitation -fossil-poor peloidal and fenestral wackestones, calm water deposition 3. Restricted intertidal -peloidal grainstones with micritised grains, deposition in channels ripping up subtidal facies. Restricted supratidal -microbial laminites -immature palaeosols A small-scale cyclicity can be identified by the arrangement of microfacies vertically. Typical cycles show a stromatoporoid-rich base, followed by an Amphipora floatstone, capped by a fenestral fossil-poor micrite. Locally emergence is indicated by juvenile soil development or laminite deposition. Cycles are on average 2 to 3 m thick. Fischer plots have been produced to show the pattern of cycle development through time, and comparisons between sections is attempted. The mechanism causing cyclicity is as yet still unclear, with an intricate balance between autocyclic and allocyclic factors being probable

PSS8 Use of consumer market research panels to generate prevalence and disease burden estimates in data-sparse diseases: a case study in severe Chronic Hand Eczema

Farrando, Jordi;Febles, Maria Dolors ;Henrich, Jordi;Tarrasó, Olga ;Fuertes, J.C.;Pérez, S

Modulation of ligand-heme reactivity by binding pocket residues demonstrated in cytochrome c' over the femtosecond-second temporal range

The ability of hemoproteins to discriminate between diatomic molecules, and the subsequent affinity for their chosen ligand, is fundamental to the existence of life. These processes are often controlled by precise structural arrangements in proteins, with heme pocket residues driving reactivity and specificity. One such protein is cytochrome c', which has the ability to bind nitric oxide (NO) and carbon monoxide (CO) on opposite faces of the heme, a property that is shared with soluble guanylate cycle. Like soluble guanylate cyclase, cytochrome c' also excludes O completely from the binding pocket. Previous studies have shown that the NO binding mechanism is regulated by a proximal arginine residue (R124) and a distal leucine residue (L16). Here, we have investigated the roles of these residues in maintaining the affinity for NO in the heme binding environment by using various time-resolved spectroscopy techniques that span the entire femtosecond-second temporal range in the UV-vis spectrum, and the femtosecond-nanosecond range by IR spectroscopy. Our findings indicate that the tightly regulated NO rebinding events following excitation in wild-type cytochrome c' are affected in the R124A variant. In the R124A variant, vibrational and electronic changes extend continuously across all time scales (from fs-s), in contrast to wild-type cytochrome c' and the L16A variant. Based on these findings, we propose a NO (re)binding mechanism for the R124A variant of cytochrome c' that is distinct from that in wild-type cytochrome c'. In the wider context, these findings emphasize the importance of heme pocket architecture in maintaining the reactivity of hemoproteins towards their chosen ligand, and demonstrate the power of spectroscopic probes spanning a wide temporal range. © 2013 FEBS.

Combined pulsed electron double resonance EPR and molecular dynamics investigations of calmodulin suggest effects of crowding agents on protein structures

A.M.S. received Early Stage Research Funding from the European Union’s Seventh Framework Programme FP-7-PEOPLE-2013-ITN through the “MAGnetic Innovation in Catalysis” (MAGIC) Initial Training Network (grant agreement no. 606831). Part of this work was also supported by BBSRC grant: BB/M007065/1. J.L. thanks the Royal Society for a University Research Fellowship, the Carnegie Trust (RIG007510), and the Wellcome Trust for a Multi-User Equipment grant (099149/Z/12/Z).Calmodulin (CaM) is a highly dynamic Ca2+-binding protein that exhibits large conformational changes upon binding Ca2+ and target proteins. Although it is accepted that CaM exists in an equilibrium of conformational states in the absence of target protein, the physiological relevance of an elongated helical linker region in the Ca2+-replete form has been highly debated. In this study, we use PELDOR (pulsed electron–electron double resonance) EPR measurements of a doubly spin-labeled CaM variant to assess the conformational states of CaM in the apo-, Ca2+-bound, and Ca2+ plus target peptide-bound states. Our findings are consistent with a three-state conformational model of CaM, showing a semi-open apo-state, a highly extended Ca2+-replete state, and a compact target protein-bound state. Molecular dynamics simulations suggest that the presence of glycerol, and potentially other molecular crowding agents, has a profound effect on the relative stability of the different conformational states. Differing experimental conditions may explain the discrepancies in the literature regarding the observed conformational state(s) of CaM, and our PELDOR measurements show good evidence for an extended conformation of Ca2+-replete CaM similar to the one observed in early X-ray crystal structures.Publisher PDFPeer reviewe

Cosmology, Oscillating Physics and Oscilllating Biology

According to recent reports there is an excess correlation and an apparent regularity in the galaxy one-dimensional polar distribution with a characteristic scale of 128 $h^{-1}$ Mpc. This aparent spatial periodicity can be naturally explained by a time oscillation of the gravitational constant $G$. On the other hand, periodic growth features of bivalve and coral fossiles appear to show a periodic component in the time dependence of the number of days per year. In this letter we show that a time oscillating gravitational constant with similar period and amplitude can explain such a feature.Comment: 9 pages. latex using revtex. This revised version is supposed to be free of e-mail nois

Photochemical Spin Dynamics of the Vitamin B12 Derivative, Methylcobalamin

Derivatives of vitamin B12 are six-coordinate cobalt corrinoids found in humans, other animals and micro-organisms. By acting as enzymatic cofactors and photoreceptor chromophores they serve vital metabolic and photoprotective functions. Depending on the context, the chemical mechanisms of the biologically-active derivatives of B12 – methylcobalamin (MeCbl) and 5’-deoxyadenosylcobalamin (AdoCbl) – can be very different from one another. The extent to which this chemistry is tuned by the upper axial ligand, however, is not yet clear. Here, we have used a combination of time-resolved FT-EPR, magnetic field effect experiments and spin dynamic simulations to reveal that the upper axial ligand alone only results in relatively minor changes to the photochemical spin dynamics of B12. By studying the photolysis of MeCbl, we find that, much like for AdoCbl, the initial (or ‘geminate’) radical pairs are born predominantly in the singlet spin-state and thus originate from singlet excited-state precursors. This is in contrast to the triplet radical pairs and precursors proposed previously. Unlike AdoCbl, the extent of geminate recombination is limited following MeCbl photolysis, resulting in significant distortions to the FT-EPR signal caused by polarization from spin-correlated methyl-methyl radical ‘f-pairs’ formed following rapid diffusion. Despite the photophysical mechanism that precedes photolysis of MeCbl showing a wavelength-dependence, the subsequent spin dynamics appear to be largely independent of excitation wavelength, again much like for AdoCbl. Our data finally provide clarity to what in the literature to date has been a confused and contradictory picture. We conclude that, although the upper axial position of MeCbl and AdoCbl does impact their reactivity to some extent, the remarkable biochemical diversity of these fascinating molecules is most likely a result of tuning by their protein environment