Penyelesaian Tindak Pidana Perjudian yang Dilakukan oleh Anak Menurut UU No.11 Tahun 2012

The title of this legal writing is "The Completion of the Crime of Gambling Carried Out by minors based on the law Number 11 of 2012 on the Juvenile Justice system". This type of research is normative legal research. Normative legal research is a research conducted or focusing on norm of positive law in the form of legislation. Legal issues raised is whether the completion of the crime of gambling by children is in conformity with the law Number 11 of 2012 about the juvenile justice system. The purpose of this research is to determine and analyze the completion of the crime of gambling by children under the law of the juvenile justice system. The result showed that the efforts made to prevent criminal acts of a child is an attempt preventive and repressive efforts. Juvenile justice system is closely related to restorative justice. Regarding the obligation to make a diversion conducted by law enforcement officials, in particular under Article 7 and 96 of the law number 11 of 2012 on the Juvenile Justice System

Percentage of time Group I and Group II sites contacted PIP₂ during FAK-PIP₂ interactions.

<p>Percentage of time Group I and Group II sites contacted PIP₂ during FAK-PIP₂ interactions.</p

FAK adopts a set of preferential orientations toward PIP₂-containing lipid bilayers.

<p>Arrows represent the direction from the center of mass of the F2 subdomain of the FERM domain and C-lobe of the kinase domain to the COM of the F1 subdomain of the FERM domain and N-lobe of the kinase domain. Color scheme is the same as <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0132833#pone.0132833.g001" target="_blank">Fig 1</a>.</p

FAK does not actively recruit PIP₂.

<p>RDF of ions as a function of distance to PIP₂ in the presence (<i>solid line</i>) and absence (<i>dashed line</i>) of FAK. RDF of PIP₂ as a function of distance to PIP₂ in the presence (<i>dash-dotted line</i>) and absence (<i>dotted line</i>) of FAK. All distances are measured with respect to the 1’-phosphate of PIP₂. The final 900 ns of each simulation was used for analysis. Simulations II and III had very similar results and are therefore not shown.</p

Novel Phosphotidylinositol 4,5-Bisphosphate Binding Sites on Focal Adhesion Kinase

<div><p>Focal adhesion kinase (FAK) is a protein tyrosine kinase that is ubiquitously expressed, recruited to focal adhesions, and engages in a variety of cellular signaling pathways. Diverse cellular responses, such as cell migration, proliferation, and survival, are regulated by FAK. Prior to activation, FAK adopts an autoinhibited conformation in which the FERM domain binds the kinase domain, blocking access to the activation loop and substrate binding site. Activation of FAK occurs through conformational change, and acidic phospholipids such as phosphatidylinositol 4,5-bisphosphate (PIP₂) are known to facilitate this process. PIP₂ binding alters the autoinhibited conformation of the FERM and kinase domains and subsequently exposes the activation loop to phosphorylation. However, the detailed molecular mechanism of PIP₂ binding and its role in FAK activation remain unclear. In this study, we conducted coarse-grained molecular dynamics simulations to investigate the binding of FAK to PIP₂. Our simulations identified novel areas of basic residues in the kinase domain of FAK that potentially undergo transient binding to PIP₂ through electrostatic attractions. Our investigation provides a molecular picture of PIP₂-initiated FAK activation and introduces promising new pathways for future studies of FAK regulation.</p></div

FAK preferentially interacts with the PIP₂-containing bilayer leaflet.

<p>Minimal distance between FAK and DOPC leaflet with (<i>solid line</i>) and without PIP₂ (<i>dashed line</i>) in simulation I (<i>black</i>), II (red), and III (<i>green</i>)</p

Group I and II interaction sites correspond to large basic patches in FAK.

<p>a1, b1, and c1: Mapping of Group I (<i>green</i>) and Group II (<i>yellow</i>) residues onto the crystal structure of FAK (F1 (<i>violet</i>), F2 (<i>blue</i>), and F3 (<i>cyan</i>) subdomains of the FERM domain, N-lobe (red), A-loop (<i>iceblue</i>), and C-lobe (<i>magenta</i>) of the kinase domain, and linker (<i>gray</i>)). a2, b2, and c2: Electrostatic potential surface of FAK kinase calculated using APBS [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0132833#pone.0132833.ref028" target="_blank">28</a>]. The view of the electrostatic potential surface in a2, b2, and c2 corresponds to the orientation shown in a1, b1, and c1, respectively.</p

Domain structure of FAK and illustration of the simulation system.

<p>(a) The two N-terminal domains of FAK form the autoinhibited conformation and are connected via a linker. FERM domain: <i>blue</i>; kinase domain: <i>red</i>; linker: <i>green</i>. (b) FAK lies above a DOPC bilayer (<i>gray</i>) with 10% PIP₂ (<i>spheres</i>, cyan and ochre) in the upper leaflet. Ions and water molecules are omitted for clarity. All molecular graphics are rendered in VMD [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0132833#pone.0132833.ref013" target="_blank">13</a>].</p

Proteorhodopsin Activation Is Modulated by Dynamic Changes in Internal Hydration

Proteorhodopsin, a member of the microbial rhodopsin family, is a seven-transmembrane α-helical protein that functions as a light-driven proton pump. Understanding the proton-pumping mechanism of proteorhodopsin requires intimate knowledge of the proton transfer pathway via complex hydrogen-bonding networks formed by amino acid residues and internal water molecules. Here we conducted a series of microsecond time scale molecular dynamics simulations on both the dark state and the initial photoactivated state of blue proteorhodopsin to reveal the structural basis for proton transfer with respect to protein internal hydration. A complex series of dynamic hydrogen-bonding networks involving water molecules exists, facilitated by water channels and hydration sites within proteorhodopsin. High levels of hydration were discovered at each proton transfer sitethe retinal binding pocket and proton uptake and release sitesunderscoring the critical participation of water molecules in the proton-pumping mechanism. Water-bridged interactions and local water channels were also observed and can potentially mediate long-distance proton transfer between each site. The most significant phenomenon is after isomerization of retinal, an increase in water flux occurs that connects the proton release group, a conserved arginine residue, and the retinal binding pocket. Our results provide a detailed description of the internal hydration of the early photointermediates in the proteorhodopsin photocycle under alkaline pH conditions. These results lay the fundamental groundwork for understanding the intimate role that hydration plays in the structure–function relationship underlying the proteorhodopsin proton-pumping mechanism, as well as providing context for the relationship of hydration in proteorhodopsin to other microbial retinal proteins

Direct and indirect effects and 95% confidence intervals for the final model.

<p>Direct and indirect effects and 95% confidence intervals for the final model.</p