An Analysis of Risk-Assessment Driven Security Restraint Use during the Transport of Forensic Patients.

Transporting forensic psychiatric patients outside of forensic hospitals has significant risks that pose competing safety and patients' rights interests. Psychiatrists and hospital administrators have a duty to keep their staff and the community safe, but this must be carefully balanced with their obligation to uphold the civil rights and liberty interests of their patients. A critical decision in this balancing is whether to utilize security restraints during patient transportation. Addressing these competing interests while striving to safely transport forensic hospital patients to the community can be challenging as hospital staff and patient advocates may voice strong, and sometimes opposing, opinions about this debate. Very little research has been conducted about these high risk and often contentious actions. Here, we describe the process for assessing risk for violence, self-harm, and elopement prior to transportation at one state forensic hospital using a pretransport risk-assessment tool created specifically for that purpose. We then present the results of research identifying which clinical and legal factors identified by our risk-assessment tool correlate with patients being transported with restraints. We also evaluated the potential for racial/ethnic and gender biases in this transportation risk-assessment process.

Thermodynamic and kinetic insights into stop codon recognition by release factor 1.

Stop codon recognition is a crucial event during translation termination and is performed by class I release factors (RF1 and RF2 in bacterial cells). Recent crystal structures showed that stop codon recognition is achieved mainly through a network of hydrogen bonds and stacking interactions between the stop codon and conserved residues in domain II of RF1/RF2. Additionally, previous studies suggested that recognition of stop codons is coupled to proper positioning of RF1 on the ribosome, which is essential for triggering peptide release. In this study we mutated four conserved residues in Escherichia coli RF1 (Gln185, Arg186, Thr190, and Thr198) that are proposed to be critical for discriminating stop codons from sense codons. Our thermodynamic and kinetic analysis of these RF1 mutants showed that the mutations inhibited the binding of RF1 to the ribosome. However, the mutations in RF1 did not affect the rate of peptide release, showing that imperfect recognition of the stop codon does not affect the proper positioning of RF1 on the ribosome.

Histidine 197 in release factor 1 is essential for a site binding and peptide release.

Class I peptide release factors 1 and 2 (RF1 and RF2, respectively) recognize the stop codons in the ribosomal decoding center and catalyze peptidyl-tRNA hydrolysis. High-fidelity stop codon recognition by these release factors is essential for accurate peptide synthesis and ribosome recycling. X-ray crystal structures of RF1 and RF2 bound to the ribosome have identified residues in the mRNA-protein interface that appear to be critical for stop codon recognition. Especially interesting is a conserved histidine in all bacterial class I release factors that forms a stacking interaction with the second base of the stop codon. Here we analyzed the functional significance of this conserved histidine (position 197 in Escherichia coli) of RF1 by point mutagenesis to alanine. Equilibrium binding studies and transient-state kinetic analysis have shown that the histidine is essential for binding with high affinity to the ribosome. Furthermore, analysis of the binding data indicates a conformational change within the RF1·ribosome complex that results in a more tightly bound state. The rate of peptidyl-tRNA hydrolysis was also reduced significantly, more than the binding data would suggest, implying a defect in the orientation of the GGQ domain without the histidine residue.