NotesFAQContact Us
Search Tips
Peer reviewed Peer reviewed
Direct linkDirect link
ERIC Number: EJ804667
Record Type: Journal
Publication Date: 2008-Aug
Pages: 3
Abstractor: As Provided
Reference Count: 29
ISSN: ISSN-1470-8175
Teaching Noncovalent Interactions Using Protein Molecular Evolution
Fornasari, Maria Silvina; Parisi, Gustavo; Echave, Julian
Biochemistry and Molecular Biology Education, v36 n4 p284-286 Jul-Aug 2008
Noncovalent interactions and physicochemical properties of amino acids are important topics in biochemistry courses. Here, we present a computational laboratory where the capacity of each of the 20 amino acids to maintain different noncovalent interactions are used to investigate the stabilizing forces in a set of proteins coming from organisms adapted to different environments. Using protein sequence and structure information it is possible to evaluate the noncovalent contributions to the stabilization of a given protein fold. As a case study, we use the protein lumazine synthase from three different organisms adapted to live in extreme temperatures: one psychrophilic (optimal growth temperature, 0-20 degrees C), one mesophilic (optimal growth temperature, 20-50 degrees C), and one thermophilic (optimal growth temperature, 80-110 degrees C). We found that this computational laboratory for biochemistry and molecular biology courses enhances student amino acid noncovalent interaction understanding and how these interactions are involved in protein stability. (Contains 1 figure.)
John Wiley & Sons, Inc. Subscription Department, 111 River Street, Hoboken, NJ 07030-5774. Tel: 800-825-7550; Tel: 201-748-6645; Fax: 201-748-6021; e-mail:; Web site:
Publication Type: Journal Articles; Reports - Descriptive
Education Level: N/A
Audience: Teachers
Language: English
Sponsor: N/A
Authoring Institution: N/A