Protein design and folding: template trapping of self-assembled helical bundles

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...

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Bibliographic Details
Published in:Journal of peptide science 2001-03, Vol.7 (3), p.146-151
Main Authors: Grell, Daniel, Richardson, Jane S., Mutter, Manfred
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Chemical Phenomena
Chemistry, Physical
Chromatography, High Pressure Liquid
Circular Dichroism
Combinatorial Chemistry Techniques
complementary packing
Models, Chemical
Models, Molecular
Molecular Sequence Data
Protein Binding
protein design
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins - chemical synthesis
Proteins - chemistry
self-assembly
Spectrometry, Mass, Electrospray Ionization
Template Assembled Synthetic Proteins
template trapping
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Summary: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.
ISSN:1075-2617
1099-1387
DOI:10.1002/psc.308