Test environment running 7.6.6

Cultural advice

The Australian National University acknowledges, celebrates and pays our respects to the Ngunnawal and Ngambri people of the Canberra region and to all First Nations Australians on whose traditional lands we meet and work, and whose cultures are among the oldest continuing cultures in human history.

Aboriginal and Torres Strait Islander peoples are advised that ANU Library collections may include images, names, voices, and other representations of deceased persons.

Material in the collection may contain terms, language or views that reflect the period in which the item was created and may be considered inappropriate today.

NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach

Loading...
Thumbnail Image

Date

Authors

Guignard, Laurent
Ozawa, Kiyoshi
Pursglove, Sharon
Otting, Gottfried
Dixon, Nicholas

Journal Title

Journal ISSN

Volume Title

Publisher

Elsevier

Abstract

A cell-free protein expression system was established that provides protein samples of adequate concentration and purity for direct NMR analysis. The Escherichia coli peptidyl-prolyl cis-trans isomerase PpiB was expressed in this system with dual amino acid-selective isotope labeling to identify the NMR signal from the active site-residue Arg87. Addition of the substrate succinyl-Ala-Ala-Pro-Phe-p-nitroanilide selectively shifted its15N-HSQC cross peak, confirming binding to the active site. As cell-free protein expression provides high yields of protein per unit mass of labeled amino acid and sample handling is minimal, this strategy presents an exceptionally inexpensive and rapid approach to protein analysis.

Description

Citation

Source

FEBS Letters

Book Title

Entity type

Access Statement

License Rights

Restricted until

2037-12-31