ERIC Number: EJ1202311
Record Type: Journal
Publication Date: 2019
Pages: 9
Abstractor: As Provided
ISBN: N/A
ISSN: ISSN-1470-8175
EISSN: N/A
Available Date: N/A
Guided Inquiry Activity Linking Thermodynamic Parameters of Protein Unfolding to Structure Using Differential Scanning Fluorimetry Data in the Biophysical Chemistry Classroom
Emery, Patrick; Yezierski, Ellen J.; Page, Richard C.
Biochemistry and Molecular Biology Education, v47 n1 p67-75 Jan-Feb 2019
Visualizations are useful tools for helping students to understand chemistry concepts at the particulate level. A classroom activity was developed based on learning theory and evidence-based practices, combining protein visualization with thermodynamic parameters from differential scanning fluorimetry (DSF) data analysis. Coding of student responses showed that many students were able to establish the desired connections among protein structure, thermodynamic parameters, and experimental data analysis, while a few did not recognize all the differences between the folded and unfolded forms of the protein. The activity elicits student prior knowledge through the pre-class activity, has the students examine the interactions within a protein molecule through the PyMOL activity, introduces DSF analysis using the learning cycle through the Guided Inquiry activity, and tests student learning through the post-class activity. Upon completing the activity, the majority of students successfully met the learning goals.
Descriptors: Visualization, Chemistry, Scientific Concepts, Concept Formation, Learning Activities, Thermodynamics, Science Activities, Prior Learning, Molecular Structure, Inquiry
Wiley-Blackwell. 350 Main Street, Malden, MA 02148. Tel: 800-835-6770; Tel: 781-388-8598; Fax: 781-388-8232; e-mail: cs-journals@wiley.com; Web site: http://www.wiley.com/WileyCDA
Publication Type: Journal Articles; Reports - Descriptive
Education Level: N/A
Audience: N/A
Language: English
Sponsor: National Science Foundation (NSF); National Institutes of Health (DHHS)
Authoring Institution: N/A
Grant or Contract Numbers: MCB1552113; R35GM128595
Author Affiliations: N/A