RESUMO
In a study to assess law enforcement officers' perceptions of rape and rape victims, researchers asked 149 law enforcement officers to respond to surveys which included a definition of rape measure, an unfounded rape claims measure, and the Rape Myth Acceptance Scale-Revised (RMA-R) measure. Although most officers scored low on the RMA-R--indicating that they did not adhere to myths about rape--most officers also responded with incomplete definitions of rape and inaccurate estimates of the number of false rape claims. Multivariate analyses indicated that officers' open-ended responses did not predict their scores on the RMA-R scale. It is argued that the RMA-R alone does not accurately measure officers' understanding of rape. Officers need ongoing training on the legal elements of the crime, the necessity of sensitivity with victims, and research-based statistics on the prevalence of rape.
Assuntos
Vítimas de Crime/legislação & jurisprudência , Defesa do Paciente/legislação & jurisprudência , Polícia/legislação & jurisprudência , Estupro/legislação & jurisprudência , Percepção Social , Adulto , Vítimas de Crime/psicologia , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Defesa do Paciente/psicologia , Preconceito , Estupro/psicologia , Estereotipagem , Inquéritos e Questionários , Adulto JovemRESUMO
Personalized cancer care requires molecular characterization of neoplasms. While the research community accepts frozen tissues as the gold standard analyte for molecular assays, the source of tissue for testing in clinical cancer care comes almost universally from formalin-fixed, paraffin-embedded tissue (FFPE). As newer technologies emerge for DNA characterization that requires higher molecular weight DNA, it was necessary to compare the quality of DNA in terms of DNA length between FFPE and cryopreserved samples. We hypothesized that cryopreserved samples would yield higher quantity and superior quality DNA compared to FFPE samples. We analyzed DNA metrics by performing a head-to-head comparison between FFPE and cryopreserved samples from 38 human tumors representing various cancer types. DNA quantity and purity were measured by UV spectrophotometry, and DNA from cryopreserved tissue demonstrated a 4.2-fold increase in DNA yield per mg of tissue (p-value < 0.001). DNA quality was measured on a fragment microelectrophoresis analyzer, and again, DNA from cryopreserved tissue demonstrated a 223% increase in the DNA quality number and a 9-fold increase in DNA fragments > 40,000 bp (p-value < 0.0001). DNA from the cryopreserved tissues was superior to the DNA from FFPE samples in terms of DNA yield and quality.
Assuntos
Criopreservação , Neoplasias , Inclusão em Parafina , Humanos , Criopreservação/métodos , Inclusão em Parafina/métodos , Neoplasias/genética , Fixação de Tecidos/métodos , DNA/análise , Formaldeído , DNA de Neoplasias/análiseRESUMO
Kinetic stability, defined as the rate of protein unfolding, is central to determining the functional lifetime of proteins, both in nature and in wide-ranging medical and biotechnological applications. Further, high kinetic stability is generally correlated with high resistance against chemical and thermal denaturation, as well as proteolytic degradation. Despite its significance, specific mechanisms governing kinetic stability remain largely unknown, and few studies address the rational design of kinetic stability. Here, we describe a method for designing protein kinetic stability that uses protein long-range order, absolute contact order, and simulated free energy barriers of unfolding to quantitatively analyze and predict unfolding kinetics. We analyze two ß-trefoil proteins: hisactophilin, a quasi-three-fold symmetric natural protein with moderate stability, and ThreeFoil, a designed three-fold symmetric protein with extremely high kinetic stability. The quantitative analysis identifies marked differences in long-range interactions across the protein hydrophobic cores that partially account for the differences in kinetic stability. Swapping the core interactions of ThreeFoil into hisactophilin increases kinetic stability with close agreement between predicted and experimentally measured unfolding rates. These results demonstrate the predictive power of readily applied measures of protein topology for altering kinetic stability and recommend core engineering as a tractable target for rationally designing kinetic stability that may be widely applicable.