Forster Resonance Energy Transfer and Conformational Stability of Proteins: An Advanced Biophysical Module for Physical Chemistry Students

Autor/inn/en	Sanchez, Katheryn M.; Schlamadinger, Diana E.; Gable, Jonathan E.; Kim, Judy E.
Titel	Forster Resonance Energy Transfer and Conformational Stability of Proteins: An Advanced Biophysical Module for Physical Chemistry Students
Quelle	In: Journal of Chemical Education, 85 (2008) 9, S.1253-1256 (4 Seiten)Infoseite zur Zeitschrift PDF als Volltext Verfügbarkeit
Sprache	englisch
Dokumenttyp	gedruckt; online; Zeitschriftenaufsatz
ISSN	0021-9584
Schlagwörter	Spectroscopy; Physics; Chemistry; Biophysics; Energy; Measurement; Thermodynamics; Theories; College Science; Laboratory Experiments; Advanced Courses; Hands on Science; Undergraduate Study + Suchen Sie Ihr Suchwort? Spektroskopie; Physik; Chemie; Biophysik; Energie; Messverfahren; Thermodynamik; Theory; Theorie; Laboratory work; Laborarbeit; Fortgeschrittenenunterricht; Grundstudium
Abstract	Protein folding is an exploding area of research in biophysics and physical chemistry. Here, we describe the integration of several techniques, including absorption spectroscopy, fluorescence spectroscopy, and Forster resonance energy transfer (FRET) measurements, to probe important topics in protein folding. Cytochrome c is used as a model protein; comparison of conformational stabilities ([delta]G[subscript H[subscript 2]O]) measured via two chemical denaturants, urea and guanidinium hydrochloride, illustrate important concepts in protein folding and intermolecular interactions. In addition, the determination of intraprotein distances based upon the FRET pair Trp-59 and the heme group for unfolded states of cytochrome c highlights the evolution of the protein structure under unfolding conditions. Analysis and discussion of these results provide opportunities to gain in-depth understanding of models for protein folding while enhancing students' skills with optical techniques. Collectively, the combination of optical spectroscopy, rigorous quantitative analysis, and a focus on biophysics illustrates the significance of fundamental research at the growing intersection of chemistry, biology, and physics. (Contains 4 figures.) (As Provided).
Anmerkungen	Division of Chemical Education of the American Chemical Society. Subscription Department, P.O. Box 1267, Bellmawr, NJ 08099-1267. Tel: 800-691-9846; Tel: 856-931-5825; Fax: 856-931-4115; e-mail: jchemed@egpp.com; Web site: http://www.jce.divched.org
Erfasst von	ERIC (Education Resources Information Center), Washington, DC
Update	2017/4/10