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ERIC Number: EJ920087
Record Type: Journal
Publication Date: 2010-Sep
Pages: 4
Abstractor: As Provided
Reference Count: 18
ISSN: ISSN-0021-9584
Quenching of Tryptophan Fluorescence in Unfolded Cytochrome "c": A Biophysics Experiment for Physical Chemistry Students
Schlamadinger, Diana E.; Kats, Dina I.; Kim, Judy E.
Journal of Chemical Education, v87 n9 p961-964 Sep 2010
Laboratory experiments that focus on protein folding provide excellent opportunities for undergraduate students to learn important topics in the expanding interdisciplinary field of biophysics. Here, we describe the use of Stern-Volmer plots to determine the extent of solvent accessibility of the single tryptophan residue (trp-59) in unfolded and partially unfolded states of the well-studied protein cytochrome "c" (cyt "c"). Comparison of quenching efficiencies for free tryptophan in solution and partially buried in cyt "c" highlights the persistence of residual structure in unfolded proteins and deepens students' understanding of protein structures and dynamics. The experiment builds on our previous laboratory module that probed thermodynamics and structures of cyt "c"; collectively, these protein-folding experiments and related topics provide physical chemistry students with opportunities to explore a comprehensive set of spectroscopy and biophysics tools. (Contains 3 figures and 1 table.)
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:; Web site:
Publication Type: Journal Articles; Reports - Research
Education Level: Higher Education
Audience: N/A
Language: English
Sponsor: N/A
Authoring Institution: N/A