Protein Folding and Stability Using Denaturants

Timothy O. Street, Naomi Courtemanche, Doug Barrick

Research output: Chapter in Book/Report/Conference proceedingChapter

52 Scopus citations


Measurements of protein folding and thermodynamic stability provide insight into the forces and energetics that determine structure, and can inform on protein domain organization, interdomain interactions, and effects of mutations on structure. This chapter describes methods, theory, and data analysis for the most accessible means to determine the thermodynamics of protein folding: chemical denaturation. Topics include overall features of the folding reaction, advances in instrumentation, optimization of reagent purity, mechanistic models for analysis, and statistical and structural interpretation of fitted thermodynamic parameters. Examples in which stability measurements have provided insight into structure and function will be taken from studies in the author's laboratory on the Notch signaling pathway. It is hoped that this chapter will enable molecular, cell, and structural biologists to make precise measurements of protein stability, and will also provide a strong foundation for biophysics students who wish to undertake experimental studies of protein folding.

Original languageEnglish (US)
Title of host publicationBiophysical Tools for Biologists, Volume One
Subtitle of host publicationIn Vitro Techniques
EditorsJohn Correi, William Detrich, III
Number of pages31
StatePublished - 2008
Externally publishedYes

Publication series

NameMethods in Cell Biology
ISSN (Print)0091-679X


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