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.

Use of electrospray ionization mass spectrometry to study binding interactions between a replication terminator protein and DNA

Thumbnail Image

Date

2002

Authors

Kapur, Amit
Beck, Jennifer
Brown, Susan Elizabeth
Dixon, Nicholas
Sheil, Margaret

Journal Title

Journal ISSN

Volume Title

Publisher

Cold Spring Harbor Laboratory Press

Abstract

Tus protein binds tightly to specific DNA sequences (Ter) on the Escherichia coli chromosome halting replication. We report here conditions for detecting the 1 : 1 Tus-Ter complex by electrospray ionization mass spectrometry (ESI-MS). ESI mass spectra of

Description

Keywords

Keywords: ammonium acetate; DNA; mutant protein; regulator protein; Tus protein; unclassified drug; article; binding affinity; dissociation constant; DNA replication; DNA sequence; mass spectrometry; pH; priority journal; protein DNA interaction; Acetates; Base Seq Dissociation constant; DNA replication; Electrospray ionization mass spectrometry; Noncovalent complex; Tus

Citation

URI

http://hdl.handle.net/1885/73338

Collections

Open Access Research

Source

Protein Science

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

10.1110/ps.ps.27702

Restricted until

DSpace software copyright © 2002-2026 LYRASIS