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

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: Contribution to conference › Paper › peer-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 language	English (US)
Pages	401-402
Number of pages	2
State	Published - 2002
Externally published	Yes
Event	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002

Other

Other	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/Territory	United States
City	Orlando, FL
Period	06/2/02 → 06/6/02

ASJC Scopus subject areas

Spectroscopy

Cite this

@conference{a1f26ed36d2a4f89a97941ba61468940,

title = "Use of electrospray ionization mass spectrometry to study binding interactions between subunits of DNA polvmerase III",

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.",

author = "Rajesh Gupta and Beck, {Jennifer L.} and Samir Hamdan and Dixon, {Nicholas E.} and Sheil, {Margaret M.}",

year = "2002",

language = "English (US)",

pages = "401--402",

note = "Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics ; Conference date: 02-06-2002 Through 06-06-2002",

}

Use of electrospray ionization mass spectrometry to study binding interactions between subunits of DNA polvmerase III. / Gupta, Rajesh; Beck, Jennifer L.; Hamdan, Samir et al.
2002. 401-402 Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

Research output: Contribution to conference › Paper › peer-review

TY - CONF

T1 - Use of electrospray ionization mass spectrometry to study binding interactions between subunits of DNA polvmerase III

AU - Gupta, Rajesh

AU - Beck, Jennifer L.

AU - Hamdan, Samir

AU - Dixon, Nicholas E.

AU - Sheil, Margaret M.

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=2442641743&partnerID=8YFLogxK

M3 - Paper

AN - SCOPUS:2442641743

SP - 401

EP - 402

T2 - Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics

Y2 - 2 June 2002 through 6 June 2002

ER -

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

Abstract

Other

ASJC Scopus subject areas

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