direkt zum Inhalt springen

direkt zum Hauptnavigationsmenü

Sie sind hier

TU Berlin

Page Content


Search for publications

all Publications (Reviews, Articles, Meetings and Proceedings)

De novo design and characterization of copper centers in synthetic four-helix-bundle proteins
Citation key ISI:000167631400010
Author Schnepf, R and Horth, P and Bill, E and Wieghardt, K and Hildebrandt, P and Haehnel, W
Pages 2186-2195
Year 2001
ISSN 0002-7863
DOI 10.1021/ja001880k
Address 1155 16TH ST, NW, WASHINGTON, DC 20036 USA
Journal J. Am. Chem. Soc
Volume 123
Number 10
Month MAR 14
Abstract The design and chemical synthesis of de novo metalloproteins on cellulose membranes with the structure of an antiparallel four-helix bundle is described. All possible combinations of three different sets of amphiphilic helices were assembled on cyclic peptide templates which were bound by a cleavable linker to the cellulose. In the hydrophobic interior, the four-helix bundle proteins carry a cysteine and several histidines at various positions for copper ligation. This approach was used successfully to synthesize, for the first time, copper proteins based on a four-helix. bundle. UV-vis spectra monitored on the solid support showed ligation of copper(II) by about one-third out of the 96 synthesized proteins and tetrahedral complexes of cobalt(II) by most of these proteins. Three of the most stable copper-binding proteins were synthesized in solution and their structural properties analyzed by spectroscopic methods. Circular dichroism, one-dimensional NMR, and size-exclusion chromatography indicate a folding into a compact state containing a high degree of secondary structure with a reasonably ordered hydrophobic core. They displayed UV-vis absorption, resonance Raman, and EPR spectra intermediate between those of type and type 2 copper centers. The present approach provides a sound basis for further optimizing the copper binding and its functional properties by using combinatorial protein chemistry guided by rational principles.
Bibtex Type of Publication Article
Download Bibtex entry

Zusatzinformationen / Extras

Quick Access:

Schnellnavigation zur Seite über Nummerneingabe

This site uses Matomo for anonymized webanalysis. Visit Data Privacy for more information and opt-out options.