The benzimidazole moiety in the title mol­ecule, C19H25N5O, is almost planar and oriented nearly perpendicular to the triazole ring. In the crystal, C—H⋯O hydrogen bonds link the mol­ecules into a network structure. There are no π–π inter­actions present but two weak C—H⋯π(ring) inter­actions are observed. A Hirshfeld surface analysis of the crystal structure indicates that the most important contributions for the crystal packing are from H⋯H (62.0%), H⋯C/C⋯H (16.1%), H⋯N/N⋯H (13.7%) and H⋯O/O⋯H (7.5%) inter­actions. Evaluation of the electrostatic, dispersion and total energy frameworks indicate that the stabilization is dominated via the dispersion energy contributions in the title compound.

The title mol­ecule, C25H23BrN2O2, adopts a cup shaped conformation with the distinctly ruffled imidazolidine ring as the base. In the crystal, weak C—H⋯O hydrogen bonds and C—H⋯π(ring) inter­actions form helical chains of mol­ecules extending along the b-axis direction that are linked by additional weak C—H⋯π(ring) inter­actions across inversion centres. The Hirshfeld surface analysis of the crystal structure indicates that the most important contributions for the crystal packing are from H⋯H (51.0%), C⋯H/H⋯C (21.3%), Br⋯H/H⋯Br (12.8%) and O⋯H/H⋯O (12.4%) inter­actions. The volume of the crystal voids and the percentage of free space were calculated to be 251.24 Å3 and 11.71%, respectively, showing that there is no large cavity in the crystal packing. Evaluation of the electrostatic, dispersion and total energy frameworks indicate that the stabilization is dominated by the dispersion energy.

A host–guest supra­molecular inclusion complex was obtained from the co-crystallization of A1/A2-bromo­but­oxy-hy­droxy difunctionalized pillar[5]arene (PilButBrOH) with adipo­nitrile (ADN), C47H53.18Br0.82O10·C6H8N2. The adipo­nitrile guest is stabilized within the electron-rich cavity of the pillar[5]arene host via multiple C—H⋯O and C—H⋯π inter­actions. Both functional groups on the macrocyclic rim are engaged in supra­molecular inter­actions with an adjacent inclusion complex via hydrogen-bonding (O—H⋯N or C—H⋯Br) inter­actions, resulting in the formation of a supra­molecular dimer in the crystal structure.

With the emergence of ultrafast X-ray sources, interest in following fast processes in small molecules and macromolecules has increased. Most of the current research into ultrafast structural dynamics of macromolecules uses X-ray free-electron lasers. In parallel, small-scale laboratory-based laser-driven ultrafast X-ray sources are emerging. Continuous development of these sources is underway, and as a result many exciting applications are being reported. However, because of their low flux, such sources are not commonly used to study the structural dynamics of macromolecules. This article examines the feasibility of time-resolved powder diffraction of macromolecular microcrystals using a laboratory-scale laser-driven ultrafast X-ray source.

The first Federation of European Biochemical Societies Advanced Course on macromolecular crystallization was launched in the Czech Republic in October 2004. Over the past two decades, the course has developed into a distinguished event, attracting students, early career postdoctoral researchers and lecturers. The course topics include protein purification, characterization and crystallization, covering the latest advances in the field of structural biology. The many hands-on practical exercises enable a close interaction between students and teachers and offer the opportunity for students to crystallize their own proteins. The course has a broad and lasting impact on the scientific community as participants return to their home laboratories and act as nuclei by communicating and implementing their newly acquired knowledge and skills.

X-ray scattering has become a major tool in the structural characterization of nanoscale materials. Thanks to the widely available experimental and computational atomic models, coordinate-based X-ray scattering simulation has played a crucial role in data interpretation in the past two decades. However, simulation of real-space pair distance distribution functions (PDDFs) from small- and wide-angle X-ray scattering, SAXS/WAXS, has been relatively less exploited. This study presents a comparison of PDDF simulation methods, which are applied to molecular structures that range in size from β-cyclo­dextrin [1 kDa molecular weight (MW), 66 non-hydrogen atoms] to the satellite tobacco mosaic virus capsid (1.1 MDa MW, 81 960 non-hydrogen atoms). The results demonstrate the power of interpretation of experimental SAXS/WAXS from the real-space view, particularly by providing a more intuitive method for understanding of partial structure contributions. Furthermore, the computational efficiency of PDDF simulation algorithms makes them attractive as approaches for the analysis of large nanoscale materials and biological assemblies. The simulation methods demonstrated in this article have been implemented in stand-alone software, SolX 3.0, which is available to download from https://12idb.xray.aps.anl.gov/solx.html.

VMXm joins the suite of operational macromolecular crystallography beamlines at Diamond Light Source. It has been designed to optimize rotation data collections from protein crystals less than 10 µm and down to below 1 µm in size. The beamline has a fully focused beam of 0.3 × 2.3 µm (vertical × horizontal) with a tuneable energy range (6–28 keV) and high flux (1.6 × 1012 photons s−1 at 12.5 keV). The crystals are housed within a vacuum chamber to minimize background scatter from air. Crystals are plunge-cooled on cryo-electron microscopy grids, allowing much of the liquid surrounding the crystals to be removed. These factors improve the signal-to-noise during data collection and the lifetime of the microcrystals can be prolonged by exploiting photoelectron escape. A novel in vacuo sample environment has been designed which also houses a scanning electron microscope to aid with sample visualization. This combination of features at VMXm allows measurements at the physical limits of X-ray crystallography on biomacromolecules to be explored and exploited.

Potentially useful biomarker tests for molecularly targeted therapies are not being adopted appropriately into clinical practice because of a lack of common evidentiary standards necessary for regulatory, reimbursement, and treatment decisions, says a new report by the National Academies of Sciences, Engineering, and Medicine.

The federal government should foster collaboration and decrease obstacles that can keep foreign atomic, molecular, and optical (AMO) physicists from working in the United States, if the nation is to maintain its position as leader in these fields, says a new report from the National Academies of Sciences, Engineering, and Medicine.

DNA, our genetic material, normally has the structure of a twisted rope ladder. Experts call this structure a double helix. Among other things, it is stabilized by stacking forces between base pairs. Scientists at the Technical University of Munich (TUM) have succeeded at measuring these forces for the very first time on the level of single base pairs. This new knowledge could help to construct precise molecular machines out of DNA.

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Alfa Cytology has launched its leukemia research services, focusing on small molecule drug development.

Ibiyemi A. Omole, PhD, honored for expertise in data converters, power management and analog and mixed-signal integrated circuit design

Scientists have used a wealth of human proteomic, genomic, and molecular data to create a free interactive, online tool mapping some of the complexities

How can oceanic microbes help produce antibiotics? This is what a recent study published in Nature Communications hopes to address as a team of researchers

Scientists have used a wealth of human proteomic, genomic, and molecular data to create a free interactive, online tool mapping some of the complexities

Scientists have used a wealth of human proteomic, genomic, and molecular data to create a free interactive, online tool mapping some of the complexities

How can oceanic microbes help produce antibiotics? This is what a recent study published in Nature Communications hopes to address as a team of researchers

Scientists have used a wealth of human proteomic, genomic, and molecular data to create a free interactive, online tool mapping some of the complexities

It is a blustery spring day, and Mouse and Mole are very excited. They are going to go bird watching and plan to make bird books. It turns out, birds are not so easy to watch. Together, they come up with a plan to get closer to the birds.

Cerebrospinal fluid proteomics in patients with Alzheimer’s disease reveals five molecular subtypes with distinct genetic risk profiles  Nature.com

Neuron type-specific proteomics reveals distinct Shank3 proteoforms in iSPNs and dSPNs lead to striatal synaptopathy in Shank3B–/– mice | Molecular Psychiatry  Nature.com

Exploring the Molecular Therapeutic Mechanisms of Gemcitabine through Quantitative Proteomics  ACS Publications

Synaptic proteomics decode novel molecular landscape in the brain  Frontiers

Native-state proteomics of Parvalbumin interneurons identifies unique molecular signatures and vulnerabilities to early Alzheimer’s pathology  Nature.com

Molecular pixelation: spatial proteomics of single cells by sequencing  Nature.com

Decrypting the molecular basis of cellular drug phenotypes by dose-resolved expression proteomics  Nature.com

Team led by U of T Engineering designs world’s most efficient catalyst for storing energy as hydrogen by splitting water moleculesToronto, ON — We can’t control when the wind blows and when the sun shines, so finding efficient ways to store energy from alternative sources remains an urgent research problem. Now, a group of researchers led […]

El reportero estrella de 'The New Yorker' publica en España 'Cabeza de serpiente', una crónica sobre el poder de la mafia china y el lado más turbio del sueño americano Leer

Los de Chus Mateo han perdido todos sus partidos lejos del Wizink, desapareciendo en los últimos cuartos alarmantemente. El domingo visitan Murcia en ACB y el jueves al Armani en Euroliga. Lesión de Musa Leer

See how how many seasonal pop-ups you can hit this month, as we give you a great tip on finding the perfect gift at a holiday market near you.

The post Holiday shopping Whac-a-Mole first appeared on Federal News Network.

The grand discovery of alien life is likely to come in the form of frustratingly subtle chemical clues.

Location: Electronic Resource- 

Location: Electronic Resource- 

Location: Electronic Resource- 

Panelistas señalaron que el gobierno pierde la oportunidad de acoger las recomendaciones y abrir diálogo; otros creen que gobierno reconocen aspectos positivos del informe.

¿Qué es la medicina ortomolecular?

I seem to remember someone here recommending a tabletop at-home device for Covid testing (maybe NAAT?) that's approved in the European market but not in the US. Can someone here remind me?

Context: We've got an ambiguous rapid antigen test result for COVID in our house. The line is so faint that it is not pink or red, although two out of three of us see something there, like a shadow. We'd hoped to confirm with PCR so we can plan (eg what are the chances we'll need to cancel our Thanksgiving trip to see my elderly mother in her nursing home?) but we learned that molecular testing isn't offered in our region anymore.

I know that I might not be able to buy anything that is immediately useful for this situation, but since Covid isn't going anywhere, maybe this is worth an investment. We do plan to follow up with more RATs over the next few days.

We do know that CDC guidelines don't require us to care. I'm not worried for my kid at all, she's only mildly ill. I just want to do the right things to limit spread, here and in future.

En 6AM Hoy por Hoy de Caracol Radio estuvo Luis Guillermo Vélez, exsuperintendente de Sociedades, para hablar sobre qué viene ahora tras ser admitida la demanda que radicaron para frenar la intervención forzosa al Hospital San Juan De Dios.

The scientific feat is also "a breakthrough for practical applications because entangled molecules can be the building blocks for many future applications.” says physicist Lawrence Cheuk.

Princeton chemists are expanding our understanding of the universe by identifying complex molecules in interstellar space.

Jacques R. Fresco, the emeritus Damon B. Pfeiffer Professor in the Life Sciences and an emeritus professor of molecular biology, died on Dec. 5. He served on Princeton's faculty for 53 years before retiring in July 2013.

Austin Newton, a founding member of the Department of Molecular Biology, established a new experimental system and mentored generations of undergraduates, graduate students and postdoctoral fellows. He died May 13 in Princeton at age 85.

The human cardiovascular system has adapted to function optimally in Earth's 1G gravity, and microgravity conditions cause myocardial abnormalities, including atrophy and dysfunction. However, the underlying mechanisms linking microgravity and cardiac anomalies are incompletely understood. In this study, we investigated whether and how calpain activation promotes myocardial abnormalities under simulated microgravity conditions. Simulated microgravity was induced by tail suspension in mice with cardiomyocyte-specific deletion of Capns1, which disrupts activity and stability of calpain-1 and calpain-2, and their WT littermates. Tail suspension time-dependently reduced cardiomyocyte size, heart weight, and myocardial function in WT mice, and these changes were accompanied by calpain activation, NADPH oxidase activation, and oxidative stress in heart tissues. The effects of tail suspension were attenuated by deletion of Capns1. Notably, the protective effects of Capns1 deletion were associated with the prevention of phosphorylation of Ser-345 on p47phox and attenuation of ERK1/2 and p38 activation in hearts of tail-suspended mice. Using a rotary cell culture system, we simulated microgravity in cultured neonatal mouse cardiomyocytes and observed decreased total protein/DNA ratio and induced calpain activation, phosphorylation of Ser-345 on p47phox, and activation of ERK1/2 and p38, all of which were prevented by calpain inhibitor-III. Furthermore, inhibition of ERK1/2 or p38 attenuated phosphorylation of Ser-345 on p47phox in cardiomyocytes under simulated microgravity. This study demonstrates for the first time that calpain promotes NADPH oxidase activation and myocardial abnormalities under microgravity by facilitating p47phox phosphorylation via ERK1/2 and p38 pathways. Thus, calpain inhibition may be an effective therapeutic approach to reduce microgravity-induced myocardial abnormalities.

Dilated cardiomyopathy (DCM) is associated with mutations in cardiomyocyte sarcomeric proteins, including α-tropomyosin. In conjunction with troponin, tropomyosin shifts to regulate actomyosin interactions. Tropomyosin molecules overlap via tropomyosin–tropomyosin head-to-tail associations, forming a continuous strand along the thin filament. These associations are critical for propagation of tropomyosin's reconfiguration along the thin filament and key for the cooperative switching between heart muscle contraction and relaxation. Here, we tested perturbations in tropomyosin structure, biochemistry, and function caused by the DCM-linked mutation, M8R, which is located at the overlap junction. Localized and nonlocalized structural effects of the mutation were found in tropomyosin that ultimately perturb its thin filament regulatory function. Comparison of mutant and WT α-tropomyosin was carried out using in vitro motility assays, CD, actin co-sedimentation, and molecular dynamics simulations. Regulated thin filament velocity measurements showed that the presence of M8R tropomyosin decreased calcium sensitivity and thin filament cooperativity. The co-sedimentation of actin and tropomyosin showed weakening of actin-mutant tropomyosin binding. The binding of troponin T's N terminus to the actin-mutant tropomyosin complex was also weakened. CD and molecular dynamics indicate that the M8R mutation disrupts the four-helix bundle at the head-to-tail junction, leading to weaker tropomyosin–tropomyosin binding and weaker tropomyosin–actin binding. Molecular dynamics revealed that altered end-to-end bond formation has effects extending toward the central region of the tropomyosin molecule, which alter the azimuthal position of tropomyosin, likely disrupting the mutant thin filament response to calcium. These results demonstrate that mutation-induced alterations in tropomyosin–thin filament interactions underlie the altered regulatory phenotype and ultimately the pathogenesis of DCM.