Use of electrospray ionization mass spectrometry to study binding interactions between subunits of DNA polvmerase III

Rajesh Gupta*, Jennifer L. Beck, Samir Hamdan, Nicholas E. Dixon, Margaret M. Sheil

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingConference contributionpeer-review

Abstract

The binding affinity between the TusTer protein-DNA complex involved in termination of DNA replication was investigated using electrospray ionization mass spectrometry (ESI-MS). The ε186-θ complex from DNA polymerase III was prepared for ESI-MS analysis by dialysis. The X-ray structure of the complex revealed substantial polar and electrostatic interactions between binding partners. The results show stability of ε186-θ complex to be >9 M in salt solutions suggesting that hydrophobic interactions play substantial role in stability of complex.

Original languageEnglish (US)
Title of host publicationProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Pages401-402
Number of pages2
StatePublished - 2002
Externally publishedYes
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

OtherProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
CountryUnited States
CityOrlando, FL
Period06/2/0206/6/02

ASJC Scopus subject areas

  • Spectroscopy

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