The denatured state (the other half of the folding equation) and its role in protein stability
@article{Shortle1996TheDS, title={The denatured state (the other half of the folding equation) and its role in protein stability}, author={D. Shortle}, journal={The FASEB Journal}, year={1996}, volume={10}, pages={27 - 34} }
Experimental studies of the physical interactions that stabilize protein structure are complicated by the fact that proteins do not unfold to a simple reference state. When their folded structure breaks down, protein chains do not become random coils. Instead, they enter a poorly understood ensemble of partially folded states known collectively as the denatured state. Although it has long been held that agents that promote protein unfolding act specifically oh the denatured state, the idea that… CONTINUE READING
Topics from this paper
354 Citations
Experimental characterization of the denatured state ensemble of proteins.
- Chemistry, Medicine
- Methods in molecular biology
- 2009
- 11
Perturbations of the denatured state ensemble: Modeling their effects on protein stability and folding kinetics
- Chemistry, Medicine
- Protein science : a publication of the Protein Society
- 1996
- 18
Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability.
- Chemistry, Medicine
- Archives of biochemistry and biophysics
- 2008
- 43
Denatured state ensembles with the same radii of gyration can form significantly different long-range contacts.
- Chemistry, Medicine
- Biochemistry
- 2014
- 15
Realistic modeling of the denatured states of proteins allows accurate calculations of the pH dependence of protein stability.
- Chemistry, Medicine
- Journal of molecular biology
- 1999
- 83
Simulations of the structural and dynamical properties of denatured proteins: the "molten coil" state of bovine pancreatic trypsin inhibitor.
- Chemistry, Medicine
- Journal of molecular biology
- 1998
- 48
Probing the partly folded states of proteins by limited proteolysis.
- Medicine, Chemistry
- Folding & design
- 1997
- 275
Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins.
- Chemistry, Medicine
- Journal of molecular biology
- 2005
- 57
Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state.
- Chemistry, Medicine
- Journal of molecular biology
- 2004
- 90
References
SHOWING 1-10 OF 45 REFERENCES
Modeling the effects of mutations on the denatured states of proteins
- Chemistry, Medicine
- Protein science : a publication of the Protein Society
- 1992
- 110
- PDF
Mutations can cause large changes in the conformation of a denatured protein.
- Chemistry, Medicine
- Biochemistry
- 1993
- 89
Classification of acid denaturation of proteins: intermediates and unfolded states.
- Chemistry, Medicine
- Biochemistry
- 1994
- 342
- PDF
Principles of protein folding — A perspective from simple exact models
- Chemistry, Medicine
- Protein science : a publication of the Protein Society
- 1995
- 1,304
- PDF
Structural and energetic consequences of disruptive mutations in a protein core.
- Biology, Medicine
- Biochemistry
- 1992
- 151
Mutational studies of protein structures and their stabilities.
- Chemistry, Medicine
- Quarterly reviews of biophysics
- 1992
- 97
NMR analysis of the residual structure in the denatured state of an unusual mutant of staphylococcal nuclease.
- Chemistry, Medicine
- Structure
- 1993
- 63