| Literature DB >> 16028928 |
Tommi Kajander1, Aitziber L Cortajarena, Ewan R G Main, Simon G J Mochrie, Lynne Regan.
Abstract
The folding/unfolding transitions of a series of designed consensus tetratricopeptide repeat proteins are quantitatively described by the classical one-dimensional Ising model, which thus represents a new folding paradigm for repeat proteins. Moreover, for the first time for any protein, a theoretical model predicts the folding/unfolding transition midpoint and the width of the transition.Mesh:
Substances:
Year: 2005 PMID: 16028928 DOI: 10.1021/ja0524494
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419