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Protein design as a challenge for peptide chemists
Author(s) -
Tuchscherer Gabriele,
Mutter Manfred
Publication year - 1995
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.310010103
Subject(s) - folding (dsp implementation) , macromolecule , template , protein design , protein folding , nanotechnology , protein engineering , peptide , chemistry , computational biology , combinatorial chemistry , computer science , protein structure , materials science , biology , biochemistry , engineering , enzyme , electrical engineering
All efforts to turn the ultimate goal in protein de novo design into reality–the construction of new macromolecules with predetermined three‐dimensional structure and well‐defined functionality–failed because the mechanism of folding has still to be unravelled. In the present review, various attempts to apply synthetic tools for inducing native‐like structural features in peptides in order to bypass the folding problem are described. Besides well‐established methods for the nucleation and stabilization of secondary structures, e.g. α‐helices, β‐sheets and β‐turns, topological templates as ‘built‐in’ folding devices have more recently become the key elements for the induction of protein‐like folding units (template‐assembled synthetic proteins, TASP). Progress in the synthetic strategy and structural characterization of this new type of macromolecules opens the way for the design of functional TASP molecules.