Determining the conformational stability of a protein from urea and thermal unfolding curves

Gerald R Grimsley; Saul R Trevino; Richard L Thurlkill; J Martin Scholtz

doi:10.1002/0471140864.ps2804s71

Back

Journal article

Determining the conformational stability of a protein from urea and thermal unfolding curves

Gerald R Grimsley, Saul R Trevino, Richard L Thurlkill and J Martin Scholtz

Current protocols in protein science, Vol.71(1), pp.28.4-28.4.14

2013

DOI: 10.1002/0471140864.ps2804s71

PMID: 23377851

View Online

Abstract

This unit contains basic protocols for determining the conformational stability of a globular protein from either urea or thermal unfolding curves. Circular dichroism is the optical spectroscopic technique most commonly used to monitor protein unfolding. The protocols describe how to analyze data from an unfolding curve to obtain the thermodynamic parameters necessary to calculate conformational stability, and how to determine differences in stability between protein variants.

Algorithms

Thermodynamics

Circular Dichroism

Protein Denaturation

Protein Stability

Protein Structure, Secondary

Proteins - chemistry

Urea - chemistry

Details

Title: Subtitle: Determining the conformational stability of a protein from urea and thermal unfolding curves
Creators: Gerald R Grimsley - Texas A&M Health Science Center
Saul R Trevino - Houston Baptist University
Richard L Thurlkill - University of Louisiana at Monroe
J Martin Scholtz - Texas A&M University
Resource Type: Journal article
Publication Details: Current protocols in protein science, Vol.71(1), pp.28.4-28.4.14
DOI: 10.1002/0471140864.ps2804s71
PMID: 23377851
ISSN: 1934-3655
eISSN: 1934-3663
Language: English
Date published: 2013
Academic Unit: Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
Record Identifier: 9984288729502771

Metrics

24 Record Views