A new folding paradigm for repeat proteins

Tommi Kajander; Aitziber L Cortajarena; Ewan R G Main; Simon G J Mochrie; Lynne Regan

doi:10.1021/ja0524494

A new folding paradigm for repeat proteins

J Am Chem Soc. 2005 Jul 27;127(29):10188-90. doi: 10.1021/ja0524494.

Authors

Tommi Kajander¹, Aitziber L Cortajarena, Ewan R G Main, Simon G J Mochrie, Lynne Regan

Affiliation

¹ Department of Molecular Biophysics and Biochemistry, Physics and Applied Physics, and Chemistry, Yale University, New Haven, Connecticut 06520, USA.

PMID: 16028928
DOI: 10.1021/ja0524494

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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acid Motifs
Models, Chemical
Models, Molecular
Protein Folding*
Protein Structure, Secondary
Proteins / chemistry*
Thermodynamics

Substances

Proteins