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1.
J Microbiol Biol Educ ; 22(3)2021 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-34804323

RESUMEN

Specifications (specs) grading is a grading system in which mastery of specific educational outcomes is the basis for the final grade a student earns in the course. Implementation of the types of assessments used for specs grading has shown to be beneficial for student learning and motivation compared to traditional grading systems. We designed a specs grading strategy in an undergraduate Cell Biology course, creating 20 individual learning outcomes (LOs). The grade earned in lecture depended on the number of LOs the student mastered. If students were unable to master the content on their initial attempt, they could earn retakes for each LO assessment by completing an assignment associated with the information covered in that LO. A student's final class grade was dependent on the number of LOs mastered combined with the grade earned on their final exam. Here, we present how specifications grading was implemented in Cell Biology, differences in overall grade distribution between grading systems, improved performance on content-related assessment questions in sections using specifications grading, and more-positive attitudes for sections using specifications grading than for traditionally graded sections.

2.
Artículo en Inglés | MEDLINE | ID: mdl-32341731

RESUMEN

Georgia Gwinnett College (GGC) is an access institution with a diverse student body, located in metro Atlanta. To strengthen research skills, teach employer-valued cell biology laboratory techniques, and increase student engagement, a semester-long, inquiry-based CURE was developed and implemented in Cell Biology with Laboratory (BIOL3400K), a sophomore-level course, which serves as a "gateway" to all upper-level biology courses. This CURE centers on the investigation of a student-chosen experimental factor on the viability of cultured, mammalian cells. Through participation in this CURE, students gain experience in cell culture, fluorescence microscopy, and viability assays, and strengthen important research skills, such as literature searches, graphing, and data analyses. The impact of this CURE on student learning gains and attitudes was assessed using pre-/post-content exams and the Colorado Learning Attitudes about Science Survey (CLASS). Our data show that all students made significant content gains. Female students made larger learning gains than male students. Additionally, minority students performed better than majority students in some content areas. Student attitudes did not change, or in some cases were slightly more negative after the CURE. Overall, this CURE had a positive impact on students by engaging them in an inquiry-based laboratory experience.

3.
CBE Life Sci Educ ; 14(1): ar4, 2015 03 02.
Artículo en Inglés | MEDLINE | ID: mdl-25681416

RESUMEN

The traditional undergraduate program of study incorporates a selection of classes that represent a broad spectrum of subdisciplines. Unfortunately, few curricula successfully integrate concepts in all subdisciplines, giving undergraduates the misconception that there is a lack of application or connectedness between class subjects. An integrated course-embedded research experience (ICURE) was initiated to redress this problem by bridging classes within one discipline in an effort to engage undergraduates in a long-term analysis of biodiversity. The approach was both inclusive and longitudinal: 1) the ICURE bridge brought students from different classes and levels of instruction together with faculty members in a research project with a common goal-chronicling the changing face of the local environment in biological terms; and 2) research data collected were maintained and supplemented each semester and year in an online biodiversity database. Analysis of content and attitudinal gains suggested the integrated research protocol increased student comprehension and confidence. Results are discussed in terms of future amendments to instructional design and potential research applications. Though this program was concentrated on one discipline, there is no reason to assume other disciplines could not take advantage of similar research connections.


Asunto(s)
Investigación Biomédica/organización & administración , Curriculum , Animales , Biodiversidad , California , Código de Barras del ADN Taxonómico , Bases de Datos Factuales , Evaluación Educacional , Ambiente , Docentes , Humanos , Insectos , Internet , Modelos Educacionales , Desarrollo de Programa , Factores de Tiempo , Universidades
4.
RNA ; 10(3): 482-92, 2004 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-14970393

RESUMEN

Ribonuclease P (RNase P) is a ribozyme required for the 5' maturation of all tRNA. RNase P and the ribosome are the only known ribozymes conserved in all organisms. We set out to determine whether this ribonucleoprotein enzyme interacts with other cellular components, which may imply other functions for this conserved ribozyme. Incubation of the Bacillus subtilis RNase P holoenzyme with fractionated B. subtilis cellular extracts and purified ribosomal subunits results in the formation of a gel-shifted complex with the 30S ribosomal subunit at a binding affinity of approximately 40 nM in 0.1 M NH(4)Cl and 10 mM MgCl(2). The complex does not form with the RNase P RNA alone and is disrupted by a mRNA mimic polyuridine, but is stable in the presence of high concentrations of mature tRNA. Endogenous RNase P can also be detected in the 30S ribosomal fraction. Cleavage of a pre-tRNA substrate by the RNase P holoenzyme remains the same in the presence of the 30S ribosome, but the cleavage of an artificial non-tRNA substrate is inhibited eightfold. Hydroxyl radical protection and chemical modification identify several protected residues located in a highly conserved region in the RNase P RNA. A single mutation within this region significantly reduces binding, providing strong support on the specificity of the RNase P-30S ribosome complex. Our results also suggest that the dimeric form of the RNase P is primarily involved in 30S ribosome binding. We discuss several models on a potential function of the RNase P-30S ribosome complex.


Asunto(s)
Bacillus subtilis/enzimología , Ribonucleasa P/metabolismo , Ribosomas/metabolismo , Bacillus subtilis/química , Bacillus subtilis/metabolismo , ARN Catalítico/metabolismo , Ribonucleasa P/química , Ribosomas/química
5.
Biochemistry ; 41(43): 12986-94, 2002 Oct 29.
Artículo en Inglés | MEDLINE | ID: mdl-12390025

RESUMEN

Ribonuclease P (RNase P) is a ribonucleoprotein enzyme that catalyzes the 5' maturation of tRNA precursors. The bacterial RNase P holoenzyme is composed of a large, catalytic RNA and a small protein. Our previous work showed that Bacillus subtilis RNase P forms a specific "dimer" that contains two RNase P RNA and two RNase P protein subunits in the absence of substrate. We investigated the equilibrium and the structure of the dimeric and the monomeric holoenzyme in the absence and presence of substrates by synchrotron small-angle X-ray scattering, 3' autolytic processing, and hydroxyl radical protection. In the absence of substrate, the dimer-monomer equilibrium is sensitive to monovalent ions and the total holoenzyme concentration. At 0.1 M NH4Cl, formation of the dimer is strongly favored, whereas at 0.8 M NH4Cl, the holoenzyme is a monomer. Primary hydroxyl radical protection in the dimer is located in the specificity domain, or domain I, of the RNase P RNA. The ES complex with a substrate containing a single tRNA is always monomeric. In contrast, the dominant ES complex with a substrate containing two tRNAs is dimeric at 0.1 M NH4Cl and monomeric at 0.8 M NH4Cl. Our results show that the B. subtilis holoenzyme can be a dimer and a monomer, and the fraction of the dimer is very sensitive to the environment. Under a variety of conditions, both the holoenzyme dimer and monomer can be present in significant amounts. Because the majority of tRNA genes are organized in large operons and because of the lack of RNase E in B. subtilis, a dimeric holoenzyme may be necessary to facilitate the processing of large precursor tRNA transcripts. Alternatively, the presence of two forms of the RNase P holoenzyme may be required for other yet unknown functions.


Asunto(s)
Bacillus subtilis/enzimología , Endorribonucleasas/química , Precursores del ARN/química , ARN Bacteriano/química , ARN Catalítico/química , ARN de Transferencia/química , Secuencia de Bases , Dimerización , Holoenzimas/química , Radical Hidroxilo/química , Datos de Secuencia Molecular , Conformación de Ácido Nucleico , Unión Proteica , Estructura Terciaria de Proteína , Subunidades de Proteína , Ribonucleasa P , Dispersión de Radiación , Especificidad por Sustrato , Rayos X
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