Denatured State Effects and the Origin of Nonclassical φ Values in Protein Folding Academic Article

abstract

• Analysis of the phi value is one of the most powerful tools to understand the transition state for protein folding. In principle, phi values are expected to fall in the range of 0 to 1. However, a noticeable number of phi values have been observed which are either less than 0 or greater than 1. The origin of such phi values, sometimes referred to as noncanonical or nonclassical phi values, has been controversial. Here we show that mutational effects upon denatured state energetics can lead to nonclassical phi values.

authors

• Cho, Jae

author list (cited authors)

• Cho, J., & Raleigh, D. P.

citation count

• 40

complete list of authors

• Cho, Jae-Hyun||Raleigh, Daniel P

publication date

• January 2006

publisher

• American Chemical Society (ACS)  Publisher

published in

• Journal of the American Chemical Society  Journal

keywords

• Models, Chemical
• Protein Denaturation
• Protein Folding
• Proteins
• Reproducibility Of Results
• Thermodynamics

Digital Object Identifier (DOI)

• 10.1021/ja0669878

start page

• 16492

end page

• 16493

volume

• 128

issue

• 51

URL

• http://dx.doi.org/10.1021/ja0669878