Fault & Fracture Development in Foreland Fold and Thrust Belts - Insight from the Lurestan Province, Zagros Mountains, Iran

Second Arabian Plate Geology Workshop Abu Dhabi, UAE, 24 - 27 January 2010The Simply Folded Belt of the Zagros Mountains, Iran, represents one of the best examples of foreland fold and thrust belt. A regional fault and fracture analysis of the Cenomanian ¿ Coniacian Ilam and Sarvak formations, exposed in southern Lurestan Province, is presented as a case study for fault and fracture development in folded belts. The area is characterised by the occurrence of gentle to tight anticlines and synclines whose NW-SE axial traces are parallel to the general trend of the belt. Fold style is intimately related to both vertical and lateral facies distribution. The two formations belong to the Bangestan Group and, in this area, they represent the oldest strata exposed in the core of most anticlines outcropping at surface. Distribution, kinematics and timing of faults and fractures have been characterised through extensive fieldwork and interpretation of orthorectified QuickBird imagery and 3-D virtual outcrop models based on LiDAR technology. Data have been collected from 10 anticlines covering an area of approximately 150 x 150 km. Key outcrops for fracture and fault kinematics interpretations are presented. Field observations and interpretation of QuickBird and 3-D photorealistic models suggest a complex fault and fracture geometry and timing relationship. Both fractures and faults record pre-folding to uplift-related deformations. Pre-folding structures are typically represented by small-scale, flat-ramp-flat geometry thrusts, systematic veins and stylolites, which are superimposed on inherited syn-sedimentary normal faults. Folding-related structures generally reactivated pre-existing fracture and fault planes. Strike-slip faulting is typically recorded as the last faulting event and is probably related to late stage of fold tightening. All structures are geometrically and kinematically consistent with the trend of the Arabian passive margin and its subsequent tectonic inversion. Uplift and stress release induced opening and propagation of through-going fractures. Faults and fracture orientations generally change accordingly with local fold trend. Symmetry between fracture and fold orientation, although commonly interpreted as evidence for folding-related fracture development, is here interpreted as evidence of syn- to post-folding local vertical axis passive rotation

Molecular Dynamics of Mesophilic-Like Mutants of a Cold-Adapted Enzyme: Insights into Distal Effects Induced by the Mutations

Networks and clusters of intramolecular interactions, as well as their “communication” across the three-dimensional architecture have a prominent role in determining protein stability and function. Special attention has been dedicated to their role in thermal adaptation. In the present contribution, seven previously experimentally characterized mutants of a cold-adapted α-amylase, featuring mesophilic-like behavior, have been investigated by multiple molecular dynamics simulations, essential dynamics and analyses of correlated motions and electrostatic interactions. Our data elucidate the molecular mechanisms underlying the ability of single and multiple mutations to globally modulate dynamic properties of the cold-adapted α-amylase, including both local and complex unpredictable distal effects. Our investigation also shows, in agreement with the experimental data, that the conversion of the cold-adapted enzyme in a warm-adapted variant cannot be completely achieved by the introduction of few mutations, also providing the rationale behind these effects. Moreover, pivotal residues, which are likely to mediate the effects induced by the mutations, have been identified from our analyses, as well as a group of suitable candidates for protein engineering. In fact, a subset of residues here identified (as an isoleucine, or networks of mesophilic-like salt bridges in the proximity of the catalytic site) should be considered, in experimental studies, to get a more efficient modification of the features of the cold-adapted enzyme

Vertical-axis rotation in East Kopet Dagh, NE Iran, inferred from paleomagnetic data: oroclinal bending or complex local folding kinematics?

The Kopet Dagh Mountains in NE Iran result from Cenozoic tectonic inversion of Triassic and Jurassic rifts that formed along the southern margin of the Eurasian continental plate. The Kopet Dagh defines an arcuate orogen leading to the suggestion that oroclinal bending took place during its formation. We performed a paleomagnetic study including seven sampling sites of Paleocene formations around the Kalat syncline in the East Kopet Dagh to test whether this part of the mountain belt experienced vertical-axis rotation. Paleomagnetic measurements and a reversals test indicate that parts of the collected samples may have been partially remagnetized. Overall paleomagnetic directions of all sample sites show a mean declination of 12.5°, which is the expected direction for stable Europe in the Paleocene and therefore negates any rotation related to regional tectonic events. Directions calculated only from reversely polarized paleomagnetic data, however, suggest clockwise vertical-axis rotations up to 21° since the Paleocene. Numerical modelling of a viscous multi-layer folding mimicking the Kalat syncline stratigraphy suggests that local deviations in overprinted site-mean directions and orientation of the maximum axes of the AMS ellipsoid may be related to complex folding kinematics, acquired after regional vertical-axis rotation, where related viscous flow of relatively weak interlayer is represented by the sampled Paleocene formation. © 2019, Swiss Geological Society.This work has been supported by Swiss National Science Foundation (Grant Number 2-77297-15).Peer reviewe

Diverse approaches for the design cytosolic 5’-nucleotidase inhibitors

International audienc

Structural determinants increasing flexibility confer cold adaptation in psychrophilic phosphoglycerate kinase

International audienc

Diverse approaches for the design cytosolic 5’-nucleotidase inhibitors

International audienc

Tertiary and quaternary structure organization in gmp synthetases: implications for catalysis

Glutamine amidotransferases, enzymes that transfer nitrogen from Gln to various cellular metabolites, are modular, with the amidotransferase (GATase) domain hydrolyzing Gln, generating ammonia and the acceptor domain catalyzing the addition of nitrogen onto its cognate substrate. GMP synthetase (GMPS), an enzyme in the de novo purine nucleotide biosynthetic pathway, is a glutamine amidotransferase that catalyzes the synthesis of GMP from XMP. The reaction involves activation of XMP though adenylation by ATP in the ATP pyrophosphatase (ATPPase) active site, followed by channeling and attack of NH3 generated in the GATase pocket. This complex chemistry entails co-ordination of activity across the active sites, allosteric activation of the GATase domain to modulate Gln hydrolysis and channeling of ammonia from the GATase to the acceptor active site. Functional GMPS dimers associate through the dimerization domain. The crystal structure of the Gln-bound complex of Plasmodium falciparum GMPS (PfGMPS) for the first time revealed large-scale domain rotation to be associated with catalysis and leading to the juxtaposition of two otherwise spatially distal cysteinyl (C113/C337) residues. In this manuscript, we report on an unusual structural variation in the crystal structure of the C89A/C113A PfGMPS double mutant, wherein a larger degree of domain rotation has led to the dissociation of the dimeric structure. Furthermore, we report a hitherto overlooked signature motif tightly related to catalysis.</p