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Measuring globular protein stability

JEFFREY K. MYERS1*, SAUL R. TREVINO2
*Corresponding author
1. Davidson College, Department of Chemistry Box 7120 Davidson, NC 28035-7120, USA
2. Houston Baptist University Department of Chemistry Houston, TX 77074, USA

Abstract

Most proteins fold to specifi c native conformationsin order to function. Conformational stability is athermodynamic quantity which refl ects the populationof protein in its native, functional state. We reviewexperimental measurements of the stability of foldedconformations of proteins. Globular protein stability is animportant factor that can limit the usefulness of proteinsas pharmaceuticals or in biotechnology applications.