ArticleArchives of biochemistry and biophysics2008
Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability.
Article in Archives of biochemistry and biophysics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Helical Propensity Affects the Conformational Properties of the Denatured State of Cytochrome c'.Biophysical journal · 2018Article
- Effect of an Imposed Contact on Secondary Structure in the Denatured State of Yeast Iso-1-cytochrome c.Biochemistry · 2017Article
- Molecular determinant of the effects of hydrostatic pressure on protein folding stability.Nature communications · 2017Article
- Hydrodynamic Radii of Intrinsically Disordered Proteins Determined from Experimental Polyproline II Propensities.PLoS computational biology · 2016Article
- Differential dynamics of extracellular and cytoplasmic domains in denatured States of rhodopsin.Biochemistry · 2014Article
- Energetically significant networks of coupled interactions within an unfolded protein.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Rational modification of protein stability by targeting surface sites leads to complicated results.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Nonnative interactions regulate folding and switching of myristoylated protein.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Residual structure in unfolded proteins.Current opinion in structural biology · 2012Review
- Uncovering specific electrostatic interactions in the denatured states of proteins.Biophysical journal · 2010Article
- Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure.Biochemistry · 2009Article
- Thermally denatured state determines refolding in lipase: mutational analysis.Protein science : a publication of the Protein Society · 2009Article
- Protein ionizable groups: pK values and their contribution to protein stability and solubility.The Journal of biological chemistry · 2009Review
- Kinetic folding studies of the P22 tailspike beta-helix domain reveal multiple unfolded states.Biophysical chemistry · 2009Article
- Characterization of the unfolded state of repeat proteins.HFSP journal · 2008Article
- Effect of glycosylation on protein folding: a close look at thermodynamic stabilization.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
It is now recognized that the denatured state ensemble (DSE) of proteins can contain significant amounts of structure, particularly under native conditions. Well-studied examples include small units of hydrogen bonded secondary structure, particularly helices or turns as well as hydrophobic clusters. Other types of interactions are less well characterized and it has often been assumed that electrostatic interactions play at most a minor role in the DSE. However, recent studies have shown that both favorable and unfavorable electrostatic interactions can be formed in the DSE. These can include surprisingly specific non-native interactions that can even persist in the transition state for protein folding. DSE electrostatic interactions can be energetically significant and their modulation either by mutation or by varying solution conditions can have a major impact upon protein stability. pH dependent stability studies have shown that electrostatic interactions can contribute up to 4 kcal mol(-1) to the stability of the DSE.
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