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Molecular Structure from Models to Mastery: An Inquiry-Based Study of Human Insulin-Degrading Enzyme

Title: Molecular Structure from Models to Mastery: An Inquiry-Based Study of Human Insulin-Degrading Enzyme
Language: English
Authors: Michael A. Araujo; Alexandra A. Barrere; Selena-Rae Tirado; Candace E. Williams; Monica I. Strada; Benjamin J. Alper (ORCID 0000-0002-7940-9655)
Source: Journal of Chemical Education. 2022 99(12):4094-4101.
Availability: Division of Chemical Education, Inc. and ACS Publications Division of the American Chemical Society. 1155 Sixteenth Street NW, Washington, DC 20036. Tel: 800-227-5558; Tel: 202-872-4600; e-mail: eic@jce.acs.org; Web site: http://pubs.acs.org/jchemeduc
Peer Reviewed: Y
Page Count: 8
Publication Date: 2022
Document Type: Journal Articles; Reports - Research
Education Level: Higher Education; Postsecondary Education
Descriptors: Molecular Structure; Science Instruction; Science Laboratories; Science Experiments; Laboratory Experiments; Undergraduate Students; College Science; Biochemistry
DOI: 10.1021/acs.jchemed.1c01285
ISSN: 0021-9584; 1938-1328
Abstract: Using crystal structure data, site directed mutagenesis, and real-time kinetic assays, students designed, expressed, and purified engineered mutants of human insulin-degrading enzyme (IDE). Students designed their own IDE mutants following "in silico" analysis, used inverse PCR to generate mutant plasmid expression constructs, expressed mutant proteins in "E. coli", and tested their function "in vitro." Structural requirements for enzyme function were investigated. Students demonstrated a mastery of critical concepts in enzymology including principles of experimental design and evolutionary implications of enzyme structure-function relationships. Experimental methods for the analysis of macromolecular interactions and computational approaches to scientific inquiry were explored and applied. This investigation was conducted as part of the second-semester undergraduate biochemistry laboratory at Sacred Heart University.
Abstractor: As Provided
Entry Date: 2024
Accession Number: EJ1441710
Database: ERIC