Protein Denaturation and the Denatured State
Published Online: 19 SEP 2013
Copyright © 2001 John Wiley & Sons, Ltd. All rights reserved.
How to Cite
Hammarström, P. and Jonsson, B.-H. 2013. Protein Denaturation and the Denatured State. eLS. .
- Published Online: 19 SEP 2013
Protein denaturation experiments are routinely used to determine protein stability and to elucidate structural and dynamic effects of mutations, cofactors and ligands. Denatured states of proteins have gained wide interest in recent years owing to their fundamental importance in a wide variety of phenomena such as deciphering the protein folding problem and the molecular understanding of many diseases. Because the integrity of the folded protein structure is strongly affected by environmental factors denaturation is often studied by monitoring the effects of increasing temperature, changing pH or addition of chaotropic agents such as urea and guanidinium chloride. The structural and dynamical effects of denaturation are most efficiently characterised by using a combination of spectroscopic methods most notably circular dichroism, fluorescence and nuclear magnetic resonance. Amide hydrogen–deuterium exchange experiments can efficiently characterise partly unfolded protein structures.
There are many spectroscopic methods to study protein denaturation and denatured states.
Transitions between folded and denatured conformations of proteins are often highly cooperative.
Denatured states of proteins are ensembles of rapidly converting conformations on the nanosecond timescale.
Denatured states of proteins possess residual structures which often reside within hydrophobic cores.
Denatured states of proteins can be informative of the protein folding pathway.
- partly unfolded conformations;
- molten globule;
- residual structure;
- protein compactness;
- fluorescent probes;
- site-directed labelling