Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Academic Article

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.

authors

• Cho, Jae

published proceedings

• Arch Biochem Biophys

author list (cited authors)

• Cho, J., Sato, S., Horng, J., Anil, B., & Raleigh, D. P.

citation count

• 38

complete list of authors

• Cho, Jae-Hyun||Sato, Satoshi||Horng, Jia-Cherng||Anil, Burcu||Raleigh, Daniel P

publication date

• January 2008

publisher

• Elsevier  Publisher

published in

• Archives of Biochemistry and Biophysics  Journal

keywords

• Hydrogen-Ion Concentration
• Protein Denaturation
• Protein Engineering
• Protein Folding
• Ribosomal Proteins
• Static Electricity
• Thermodynamics

Digital Object Identifier (DOI)

• 10.1016/j.abb.2007.08.004

start page

• 20

end page

• 28

volume

• 469

issue

• 1

URL

• http://dx.doi.org/10.1016/j.abb.2007.08.004