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The NMR solution structure of the artificial protein M7 matches the computationally designed model

By C. Stordeur, R. Dallüge, O. Birkenmeier, H.L.J. Wienk, R. Rudolph, C. Lange and C. Lücke

Abstract

Rapid progress has been made in the field of protein design over the past couple of years. Computational design algorithms have been used to (i) stabilize naturally occurring proteins,[1][2] (ii) increase the solubility of membrane proteins,[3] and (iii) create de novo proteins that feature previously unknown structural folds.[4] Hence, computational protein design opens a multitude of possibilities to study the complex processes of protein folding and to possibly create new structures with novel functional properties. The first completely de novo designed protein TOP7 (PDB 1QYS), for example, provided the opportunity to explore the energy landscape of a protein structure that was never exposed to natural selection pressure.[5] The long-term goal of this research field is the ability to design proteins that perform the desired functions and exhibit high stability for possible application in industry and therapy

Year: 2008
OAI identifier: oai:dspace.library.uu.nl:1874/33298
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