Open AccessProtein de novo Design
Author(s) -
Gabriele Tuchscherer,
Pascal Dumy,
Manfred Mutter
Publication year - 1996
Publication title -
chimia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.387
H-Index - 55
eISSN - 2673-2424
pISSN - 0009-4293
DOI - 10.2533/chimia.1996.644
Subject(s) - template , folding (dsp implementation) , protein design , synthetic biology , copying , macromolecule , nanotechnology , computational biology , computer science , protein folding , chemistry , protein structure , biology , materials science , biochemistry , engineering , genetics , electrical engineering
The ultimate goal in protein de novo design is the construction of artificial proteins exhibiting tailor-made structural and functional properties. To create native-like macromolecules in copying nature's way has proven to be difficult because the mechanism of folding in its complexity has yet to be unraveled. In order to bypass the well-known folding problem, we have developed the concept of template assembled synthetic proteins (TASP); this meanwhile widely accepted strategy uses topological templates as 'built-in' devices for the induction of well-defined folding topologies. Progress in synthetic strategies, e.g., chemoselective ligation methods and orthogonal protection techniques open the way for the design of more complex TASP molecules featuring functional properties such as membrane channels, vaccines, catalysts, receptors, or ligands.