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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Grell, D; Richardson, JS; Mutter, M

Published Date

  • March 2001

Published In

Volume / Issue

  • 7 / 3

Start / End Page

  • 146 - 151

PubMed ID

  • 11297350

Pubmed Central ID

  • 11297350

Electronic International Standard Serial Number (EISSN)

  • 1099-1387

International Standard Serial Number (ISSN)

  • 1075-2617

Digital Object Identifier (DOI)

  • 10.1002/psc.308

Language

  • eng