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ERIC Number: EJ820833
Record Type: Journal
Publication Date: 2008
Pages: 5
Abstractor: As Provided
Reference Count: 12
ISSN: ISSN-1470-8175
Thermal and Chemical Denaturation of "Bacillus circulans" Xylanase: A Biophysical Chemistry Laboratory Module
Raabe, Richard; Gentile, Lisa
Biochemistry and Molecular Biology Education, v36 n6 p428-432 Nov-Dec 2008
A number of institutions have been, or are in the process of, modifying their biochemistry major to include some emphasis on the quantitative physical chemistry of biomolecules. Sometimes this is done as a replacement for part for the entire physical chemistry requirement, while at other institutions this is incorporated as a component into the traditional two-semester biochemistry series. The latter is the model used for biochemistry and molecular biology majors at the University of Richmond, whose second semester of biochemistry is a course entitled Proteins: Structure, Function, and Biophysics. What is described herein is a protein thermodynamics laboratory module, using the protein "Bacillus circulans" xylanase, which reinforces many lecture concepts, including: (i) the denatured (D) state ensemble of a protein can be different, depending on how it was populated; (ii) intermediate states may be detected by some spectroscopic techniques but not by others; (iii) the use and assumptions of the van't Hoff approach to calculate [Delta]H[degree], [Delta]S[degree], and [Delta]G[degree][subscript T] for thermal protein unfolding transitions; and (iv) the use and assumptions of an approach that allows determination of the Gibb's free energy of a protein unfolding transition based on the linear dependence of [Delta]G[degree] on the concentration of denaturant used. This module also requires students to design their own experimental protocols and spend time in the primary literature, both important parts of an upper division lab. (Contains 4 figures and 1 footnote.)
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Publication Type: Journal Articles; Reports - Descriptive
Education Level: Higher Education
Audience: N/A
Language: English
Sponsor: N/A
Authoring Institution: N/A