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Protein design and folding: template trapping of self‐assembled helical bundles
Author(s) -
Grell Daniel,
Richardson Jane S.,
Mutter Manfred
Publication year - 2001
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.308
Subject(s) - helix bundle , folding (dsp implementation) , chemistry , protein design , molecule , amphiphile , helix (gastropod) , self assembly , electrospray ionization , mass spectrometry , protein folding , covalent bond , bundle , crystallography , protein structure , chromatography , materials science , biochemistry , organic chemistry , snail , electrical engineering , copolymer , biology , engineering , polymer , composite material , ecology
An experimental system is described, permitting a detailed and systematic analysis of the factors governing self‐assembly of amphipathic helices, e.g. to a four‐helical bundle, a subject of major relevance for tertiary structure formation, protein folding and design. Following the Template Assembled Synthetic Proteins (TASP) approach, helices of different packing potential are competitively assembled in solution with a preformed two‐helix TASP molecule, and after equilibration are covalently attached (‘template trapping’) via chemoselective thioether formation. The quantitative analysis of the individual TASP molecules by high performance liquid chromatography (HPLC) and electrospray mass spectrometry (ES‐MS) allows the delineation of the role of complementary packing in helix bundle formation. The procedure established represents a general tool for the experimental verification of modern concepts in molecular recognition. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.