Abstract
In this chapter, the current state of knowledge of protein denatured states is reviewed. Flory's random coil model and recent theory and simulation approaches to protein denatured states are outlined. Nuclear magnetic resonance and fluorescence methods and the insights they have provided into residual secondary structure and transient tertiary interactions in the denatured state are discussed. Recent techniques that use experimental restraints to produce representative ensembles for the denatured state are presented. The thermodynamic and kinetic properties of the denatured state and their implications for folding and stability are considered. Finally, the prospects for future studies on protein denatured states are briefly summarized.
Original language | English |
---|---|
Title of host publication | Comprehensive Biophysics |
Publisher | Elsevier Inc. |
Pages | 72-114 |
Number of pages | 43 |
Volume | 3 |
ISBN (Print) | 9780080957180 |
DOIs | |
State | Published - 2012 |
Keywords
- Denatured state electrostatics
- Fluorescence resonance energy transfer
- Hydrogen exchange superprotection
- Loop formation kinetics
- Loop formation thermodynamics
- Molecular dynamics
- Paramagnetic relaxation enhancement
- Protein denatured states
- Radius of gyration
- Random coil
- Residual dipolar coupling
- Residual structure
- Scaling exponents
- Single molecule fluorescence