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Titolo:
Protein design and folding: Template trapping of self-assembled helical bundles
Autore:
Grell, D; Richardson, JS; Mutter, M;
Indirizzi:
Univ Lausanne, Inst Organ Chem, BCH Dorigny, CH-1015 Lausanne, SwitzerlandUniv Lausanne Lausanne Switzerland CH-1015 CH-1015 Lausanne, Switzerland Duke Univ, Dept Biochem, Durham, NC USA Duke Univ Durham NC USADuke Univ, Dept Biochem, Durham, NC USA
Titolo Testata:
JOURNAL OF PEPTIDE SCIENCE
fascicolo: 3, volume: 7, anno: 2001,
pagine: 146 -
SICI:
1075-2617(200103)7:3<146:PDAFTT>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
SYNTHETIC PROTEINS; AMINO-ACIDS; ROP PROTEIN; COILED-COIL; PEPTIDES; STABILIZATION; MODEL; GCN4;
Keywords:
complementary packing; protein design; protein folding; self-assembly; Template Assembled Synthetic Proteins; template trapping;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Mutter, M Univ Lausanne, Inst Organ Chem, BCH Dorigny, CH-1015 Lausanne, Switzerland Univ Lausanne Lausanne Switzerland CH-1015 usanne, Switzerland
Citazione:
D. Grell et al., "Protein design and folding: Template trapping of self-assembled helical bundles", J PEPT SCI, 7(3), 2001, pp. 146

Abstract

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 (C) 2001 European Peptide Society and John Wiley & Sons, Ltd.

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Documento generato il 03/04/20 alle ore 04:31:37