How does a simplified-sequence protein fold?

Abstract

To investigate a putatively primordial protein we have simplified the sequence of a 56-residue alpha/beta fold (the immunoglobulin-binding domain of protein G) by replacing it with polyalanine, polythreonine, and diglycine segments at regions of the sequence that in the folded structure are alpha-helical, beta-strand, and turns, respectively. Remarkably… (More)
DOI: 10.1016/j.bpj.2009.06.047

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Cite this paper

@article{Guarnera2009HowDA, title={How does a simplified-sequence protein fold?}, author={Enrico Guarnera and Riccardo Pellarin and Amedeo Caflisch}, journal={Biophysical journal}, year={2009}, volume={97 6}, pages={1737-46} }