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1.
Am J Pharm Educ ; 87(3): ajpe8991, 2023 04.
Artigo em Inglês | MEDLINE | ID: mdl-36270663

RESUMO

Objective. Few studies describe changes in students' class preparation, note-taking, and examination preparation over the course of professional school. This study aims to describe the use of these learning and study strategies by pharmacy students and to analyze changes during their education.Methods. We performed a prospective, observational cohort study of students at a single US pharmacy school from 2016-2019. Students completed an online survey on learning and study strategies at the beginning of each school year. Quantitative results were analyzed by level in pharmacy school during which the survey was completed as the primary predictor. Open-ended responses were thematically analyzed using an inductive approach.Results. We observed significant changes in strategies, including an increased use of audiovisual materials for course preparation, preference for electronic over manual notetaking, increasing use of lecture capture viewing, and increased use of peer materials in studying. Changes were generally largest between students' first (P1) and second (P2) years in pharmacy school, representing adjustments in student behaviors during the P1 year. In some cases, changes from the surveys in the P1 to P2 years were followed by a gradual return toward P1 survey levels. Three themes described students' comments: students' preferences shaped their learning strategies, their experiences guided changes in learning strategies, and they used additional strategies beyond those included in the survey items.Conclusions. Significant changes in pharmacy student study strategies occurred over the course of their education. This may represent an opportunity to promote use of more effective approaches for long-term learning.


Assuntos
Educação em Farmácia , Farmácia , Estudantes de Farmácia , Humanos , Autorrelato , Estudos Prospectivos , Educação em Farmácia/métodos , Currículo
2.
Nat Commun ; 12(1): 2641, 2021 05 11.
Artigo em Inglês | MEDLINE | ID: mdl-33976175

RESUMO

The mechanism of DNA synthesis has been inferred from static structures, but the absence of temporal information raises longstanding questions about the order of events in one of life's most central processes. Here we follow the reaction pathway of a replicative DNA polymerase using time-resolved X-ray crystallography to elucidate the order and transition between intermediates. In contrast to the canonical model, the structural changes observed in the time-lapsed images reveal a catalytic cycle in which translocation precedes catalysis. The translocation step appears to follow a push-pull mechanism where the O-O1 loop of the finger subdomain acts as a pawl to facilitate unidirectional movement along the template with conserved tyrosine residues 714 and 719 functioning as tandem gatekeepers of DNA synthesis. The structures capture the precise order of critical events that may be a general feature of enzymatic catalysis among replicative DNA polymerases.


Assuntos
DNA Polimerase I/metabolismo , Replicação do DNA , DNA Bacteriano/metabolismo , Proteínas de Escherichia coli/metabolismo , Cristalografia por Raios X , DNA Bacteriano/química , DNA Bacteriano/genética , Escherichia coli/genética , Escherichia coli/metabolismo , Modelos Genéticos , Conformação de Ácido Nucleico , Fatores de Tempo
3.
Elife ; 72018 10 19.
Artigo em Inglês | MEDLINE | ID: mdl-30338759

RESUMO

High resolution crystal structures of DNA polymerase intermediates are needed to study the mechanism of DNA synthesis in cells. Here we report five crystal structures of DNA polymerase I that capture new conformations for the polymerase translocation and nucleotide pre-insertion steps in the DNA synthesis pathway. We suggest that these new structures, along with previously solved structures, highlight the dynamic nature of the finger subdomain in the enzyme active site.


Assuntos
DNA Polimerase I/química , DNA/biossíntese , Escherichia coli/enzimologia , Biocatálise , Domínio Catalítico , Cristalografia por Raios X , DNA/química , Conformação Proteica
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