Chapter 17. Stability of Proteins
Published Online: 28 JAN 2005
DOI: 10.1002/3527602364.ch17
Copyright © 2004 Wiley-VCH Verlag GmbH & Co. KGaA
Book Title

Biocatalysis
Additional Information
How to Cite
Bommarius, A. S. and Riebel, B. R. (2005) Stability of Proteins, in Biocatalysis, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, FRG. doi: 10.1002/3527602364.ch17
Publication History
- Published Online: 28 JAN 2005
- Published Print: 28 JAN 2004
ISBN Information
Print ISBN: 9783527303441
Online ISBN: 9783527602360
- Summary
- Chapter
Keywords:
- stability of proteins;
- protein folding;
- Arrhenius law;
- thermodynamics of proteins;
- protein unfolding;
- protein deactivation;
- Lumry–Eyring equation;
- enzyme deactivation;
- protein aggregation;
- stabilization of proteins
Summary
Summary: Protein Folding, First-Order Decay, Arrhenius Law
The Protein Folding Problem
Why do Proteins Fold?
Two-State Model: Thermodynamic Stability of Proteins (Unfolding)
Protein Unfolding and Deactivation
Thermodynamics of Proteins
Three-State Model: Lumry–Eyring Equation
Enzyme Deactivation
Empirical Deactivation Model
Four-State Model: Protein Aggregation
Folding, Deactivation, and Aggregation
Model to Account for Competition between Folding and Inclusion Body Formation
Causes of Instability of Proteins: δG < 0, γ(t), A
Thermal Inactivation
Deactivation under the Influence of Stirring
Deactivation under the Influence of Gas Bubbles
Deactivation under the Influence of Aqueous/Organic Interfaces
Deactivation under the Influence of Salts and Solvents
Biotechnological Relevance of Protein Folding: Inclusion Bodies
Summary: Stabilization of Proteins
Correlation between Stability and Structure
