Modelling of the Creep-damage under the Reversed Stress States by Considering Damage Activation and Deactivation

Based on the experimental results of copper at 2500C by Murakami and Sanomura (1985), the isotropic and anisotropic damage models as well as the mechanism of the damage activation or deactivation are established and coupled in one constitutive equation. With the help of the finite element method the creep-damage behavior of copper under different stress states is simulated.The stress state under combined tension and torsion is discussed in detail. In the cases of the spontaneous reversal of the shear stress the rotation of the principal directions of the stress tensor leads to a delayed rotation of the principal strain directions, therefore, a change of the damage state (close or reopen of the micro-cracks) is induced. This phenomenon is modelled by the anisotropic damage model considering the mechanism of the damage activation and deactivation. The predictions are compared with those based on the isotropic model as well as the anisotropic model without the activation mechanism

Existence theorems in the geometrically non-linear 6-parametric theory of elastic plates

In this paper we show the existence of global minimizers for the geometrically exact, non-linear equations of elastic plates, in the framework of the general 6-parametric shell theory. A characteristic feature of this model for shells is the appearance of two independent kinematic fields: the translation vector field and the rotation tensor field (representing in total 6 independent scalar kinematic variables). For isotropic plates, we prove the existence theorem by applying the direct methods of the calculus of variations. Then, we generalize our existence result to the case of anisotropic plates. We also present a detailed comparison with a previously established Cosserat plate model.Comment: 19 pages, 1 figur

Natural and human-induced Holocene paleoenvironmental changes on the Guadiana shelf (northern Gulf of Cadiz)

Three contrasting sedimentary environments on the continental shelf off the Guadiana River (northern Gulf of Cadiz) were integrated in a chronological framework and analysed in terms of sedimentology and benthic foraminiferal assemblages to understand the Holocene paleoenvironmental evolution. The analysed environments differ in terms of their depositional regimes and benthic foraminiferal assemblages. However, a dominant fluvial origin of the sand fraction was observed in all three environments. Holocene sedimentary processes were mainly controlled by natural (sea level changes and climate variations) and human-induced processes (e.g. deforestation, agriculture) along four evolutionary stages. The three older stages were mainly influenced by natural processes, such as sea level variations and fluvial inputs, whereas the most recent stage reflects a combination of climatic- and human-induced processes. A deepening of sedimentary environments related to a period of rapid sea level rise, strongly influenced by river discharges occurred from c. 11,500 to c. 10,000 cal. yr BP. A reduction in sediment export to the shelf, as a result of the continuous and rapid sea level rise and enhanced estuary infilling reflects the second stage, from c. 10,000 to c. 5000 cal. yr BP. The beginning of the third stage, from c. 5000 to c. 1500–1000 cal. yr BP, is marked by a sea-level slowdown and the relatively stable climate and environmental conditions. The fourth stage, from c. 1500–1000 cal. yr BP to Recent times, reflects the intensification of human-induced processes and climatic variability in the Guadiana River basin. This stage also reflects modern depositional conditions, with the formation of a proximal prodeltaic wedge and a distal muddy body

Glacial‐interglacial variations in sediment organic carbon accumulation and benthic foraminiferal assemblages on the Bermuda Rise (ODP Site 1063) during MIS 13 to 10

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/94866/1/palo1807.pd

Modeling allosteric signal propagation using protein structure networks

Allosteric communication in proteins can be induced by the binding of effective ligands, mutations or covalent modifications that regulate a site distant from the perturbed region. To understand allosteric regulation, it is important to identify the remote sites that are affected by the perturbation-induced signals and how these allosteric perturbations are transmitted within the protein structure. In this study, by constructing a protein structure network and modeling signal transmission with a Markov random walk, we developed a method to estimate the signal propagation and the resulting effects. In our model, the global perturbation effects from a particular signal initiation site were estimated by calculating the expected visiting time (EVT), which describes the signal-induced effects caused by signal transmission through all possible routes. We hypothesized that the residues with high EVT values play important roles in allosteric signaling. We applied our model to two protein structures as examples, and verified the validity of our model using various types of experimental data. We also found that the hot spots in protein binding interfaces have significantly high EVT values, which suggests that they play roles in mediating signal communication between protein domains

Site-directed spin labeling measurements of nanometer distances in nucleic acids using a sequence-independent nitroxide probe

In site-directed spin labeling (SDSL), local structural and dynamic information is obtained via electron paramagnetic resonance (EPR) spectroscopy of a stable nitroxide radical attached site-specifically to a macromolecule. Analysis of electron spin dipolar interactions between pairs of nitroxides yields the inter-nitroxide distance, which provides quantitative structural information. The development of pulse EPR methods has enabled such distance measurements up to 70 Å in bio-molecules, thus opening up the possibility of SDSL global structural mapping. This study evaluates SDSL distance measurement using a nitroxide (designated as R5) that can be attached, in an efficient and cost-effective manner, to a phosphorothioate backbone position at arbitrary DNA or RNA sequences. R5 pairs were attached to selected positions of a dodecamer DNA duplex with a known NMR structure, and eight distances, ranging from 20 to 40 Å, were measured using double electron-electron resonance (DEER). The measured distances correlated strongly (R(2) = 0.98) with the predicted values calculated based on a search of sterically allowable R5 conformations in the NMR structure, thus demonstrating accurate distance measurements using R5. Furthermore, distance measurement in a 42 kD DNA was demonstrated. The results establish R5 as a sequence-independent probe for global structural mapping of DNA and DNA–protein complexes

Conformational changes and protein stability of the pro-apoptotic protein Bax

Pro-apoptotic Bax is a soluble and monomeric protein under normal physiological conditions. Upon its activation substantial structural rearrangements occur: The protein inserts into the mitochondrial outer membrane and forms higher molecular weight oligomers. Subsequently, the cells can undergo apoptosis. In our studies, we focused on the structural rearrangements of Bax during oligomerization and on the protein stability. Both protein conformations exhibit high stability against thermal denaturation, chemically induced unfolding and proteolytic processing. The oligomeric protein is stable up to 90 °C as well as in solutions of 8 M urea or 6 M guanidinium hydrochloride. Helix 9 appears accessible in the monomer but hidden in the oligomer assessed by proteolysis. Tryptophan fluorescence indicates that the environment of the C-terminal protein half becomes more apolar upon oligomerization, whereas the loop region between helices 1 and 2 gets solvent exposed

The Roles of Transmembrane Domain Helix-III during Rhodopsin Photoactivation

Background: Rhodopsin, the prototypic member of G protein-coupled receptors (GPCRs), undergoes isomerization of 11- cis-retinal to all-trans-retinal upon photoactivation. Although the basic mechanism by which rhodopsin is activated is well understood, the roles of whole transmembrane (TM) helix-III during rhodopsin photoactivation in detail are not completely clear. Principal Findings: We herein use single-cysteine mutagenesis technique to investigate conformational changes in TM helices of rhodopsin upon photoactivation. Specifically, we study changes in accessibility and reactivity of cysteine residues introduced into the TM helix-III of rhodopsin. Twenty-eight single-cysteine mutants of rhodopsin (P107C-R135C) were prepared after substitution of all natural cysteine residues (C140/C167/C185/C222/C264/C316) by alanine. The cysteine mutants were expressed in COS-1 cells and rhodopsin was purified after regeneration with 11-cis-retinal. Cysteine accessibility in these mutants was monitored by reaction with 4, 49-dithiodipyridine (4-PDS) in the dark and after illumination. Most of the mutants except for T108C, G109C, E113C, I133C, and R135C showed no reaction in the dark. Wide variation in reactivity was observed among cysteines at different positions in the sequence 108–135 after photoactivation. In particular, cysteines at position 115, 119, 121, 129, 131, 132, and 135, facing 11-cis-retinal, reacted with 4-PDS faster than neighboring amino acids. The different reaction rates of mutants with 4-PDS after photoactivation suggest that the amino acids in different positions in helix-III are exposed to aqueous environment to varying degrees. Significance: Accessibility data indicate that an aqueous/hydrophobic boundary in helix-III is near G109 and I133. The lack of reactivity in the dark and the accessibility of cysteine after photoactivation indicate an increase of water/4-PDS accessibility for certain cysteine-mutants at Helix-III during formation of Meta II. We conclude that photoactivation resulted in water-accessible at the chromophore-facing residues of Helix-III.National Institutes of Health (U.S.) (grant GM28289)National Eye Institute (Grant Grant EY11716)National Science Foundation (U.S.) (grant EIA-0225609