34 research outputs found
First-principles molecular-dynamics simulations of a hydrous silica melt: Structural properties and hydrogen diffusion mechanism
We use {\it ab initio} molecular dynamics simulations to study a sample of
liquid silica containing 3.84 wt.% HO.We find that, for temperatures of
3000 K and 3500 K,water is almost exclusively dissolved as hydroxyl groups, the
silica network is partially broken and static and dynamical properties of the
silica network change considerably upon the addition of water.Water molecules
or free O-H groups occur only at the highest temperature but are not stable and
disintegrate rapidly.Structural properties of this system are compared to those
of pure silica and sodium tetrasilicate melts at equivalent temperatures. These
comparisons confirm the picture of a partially broken tetrahedral network in
the hydrous liquid and suggest that the structure of the matrix is as much
changed by the addition of water than it is by the addition of the same amount
(in mole %) of sodium oxide. On larger length scales, correlations are
qualitatively similar but seem to be more pronounced in the hydrous silica
liquid. Finally, we study the diffusion mechanisms of the hydrogen atoms in the
melt. It turns out that HOSi triclusters and SiO dangling bonds play a
decisive role as intermediate states for the hydrogen diffusion.Comment: 25 pages, 18 figures. submitte
JAK2 mutation status, hemostatic risk factors and thrombophilic factors in essential thrombocythemia (ET) patients
The recently discovered JAK2 V617F point mutation, found in 50–60% of ET patients, has been
reported to be associated with a higher risk of thrombotic events. In this study, we explored if JAK2 V617F
mutation, or coexisting thrombophilic and hemostatic risk factors, contributed to these complications. We examined
32 patients with ET, and looked for pathogenetic JAK2 V617F mutation and prothrombotic genes mutations:
factor V Leiden, prothrombin and MTHFR. We also evaluated plasma levels of fibrinogen, factors VIII
and XII, AT, protein C, protein S and serum level of homocysteine. Urokinase concentration was assessed in
patients’ plasma as well as platelet lysates. There was no difference in the number of thrombotic complications
between ET patients with and without JAK2 mutation. However, we found a number of thrombophilic and
hemostatic risk factors that could contribute to thrombotic complications in ET patients. (Folia Histochemica et
Cytobiologica 2011; Vol. 49, No. 2, pp. 267–271
Mild hyperhomocysteinemia in patients with essential thrombocythemia (ET) and its relation with MTHFR gene mutation and folic acid concentration
In this study we assessed homocysteine level in 106 patients with ET – 80 females and 26 males, mean age 54 (23–82) and in 20 healthy persons – 6 males and 14 females, mean age 41 (31–54). We also searched for a relation between homocysteine level and MTHFR gene mutation as well as vitamin B12 and folic acid concentration. Median homocysteine serum level was higher in ET patients than in control group. Elevated homocysteine level primarily stems from folic acid deficiency rather than from the presence of MTHFR gene mutation. Median folic acid level was lower in ET patients presenting thrombotic and bleeding complications than in ET patient without vascular episodes. We concluded that folic acid substitution may not only prevent hyperhomocysteinemia but also the development of vascular complications in ET patients
Citius, Altius, Fortius—Advanced Mass Spectrometry in Service of Forensic Analysis
This review presents numerous studies in which mass spectrometry has been used to assist forensic investigation. Due to its unique capabilities, mainly high-resolution mass data and structural information, high sensitivity, and cooperation with separation techniques, this method provides access to many tools streamlining and accelerating sample analysis. Low analyte consumption, advanced derivatization procedures and availability of isotopically labeled standards offer opportunities to study materials previously not considered viable evidence, opening new avenues in forensic investigations
Veni, Vidi, Vici: Immobilized Peptide-Based Conjugates as Tools for Capture, Analysis, and Transformation
Analysis of peptide biomarkers of pathological states of the organism is often a serious challenge, due to a very complex composition of the cell and insufficient sensitivity of the current analytical methods (including mass spectrometry). One of the possible ways to overcome this problem is sample enrichment by capturing the selected components using a specific solid support. Another option is increasing the detectability of the desired compound by its selective tagging. Appropriately modified and immobilized peptides can be used for these purposes. In addition, they find application in studying the specificity and activity of proteolytic enzymes. Immobilized heterocyclic peptide conjugates may serve as metal ligands, to form complexes used as catalysts or analytical markers. In this review, we describe various applications of immobilized peptides, including selective capturing of cysteine-containing peptides, tagging of the carbonyl compounds to increase the sensitivity of their detection, enrichment of biological samples in deoxyfructosylated peptides, and fishing out of tyrosine–containing peptides by the formation of azo bond. Moreover, the use of the one-bead-one-compound peptide library for the analysis of substrate specificity and activity of caspases is described. Furthermore, the evolution of immobilization from the solid support used in peptide synthesis to nanocarriers is presented. Taken together, the examples presented here demonstrate immobilized peptides as a multifunctional tool, which can be successfully used to solve multiple analytical problems
<i>Veni, Vidi, Vici</i>: Immobilized Peptide-Based Conjugates as Tools for Capture, Analysis, and Transformation
Analysis of peptide biomarkers of pathological states of the organism is often a serious challenge, due to a very complex composition of the cell and insufficient sensitivity of the current analytical methods (including mass spectrometry). One of the possible ways to overcome this problem is sample enrichment by capturing the selected components using a specific solid support. Another option is increasing the detectability of the desired compound by its selective tagging. Appropriately modified and immobilized peptides can be used for these purposes. In addition, they find application in studying the specificity and activity of proteolytic enzymes. Immobilized heterocyclic peptide conjugates may serve as metal ligands, to form complexes used as catalysts or analytical markers. In this review, we describe various applications of immobilized peptides, including selective capturing of cysteine-containing peptides, tagging of the carbonyl compounds to increase the sensitivity of their detection, enrichment of biological samples in deoxyfructosylated peptides, and fishing out of tyrosine–containing peptides by the formation of azo bond. Moreover, the use of the one-bead-one-compound peptide library for the analysis of substrate specificity and activity of caspases is described. Furthermore, the evolution of immobilization from the solid support used in peptide synthesis to nanocarriers is presented. Taken together, the examples presented here demonstrate immobilized peptides as a multifunctional tool, which can be successfully used to solve multiple analytical problems