Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions.

Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions. Research Abstract Details 

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Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions. Abstract Text:

Xiaoting Tang,Gerhard R Munske,William F Siems,James E Bruce,

A new mass spectrometry identifiable cross-linking strategy has been developed to study protein-protein interactions. The new cross-linker was designed to have two low-energy MS/MS-cleavable bonds in the spacer chain to provide three primary benefits: First, a reporter tag can be released from cross-link due to cleavage of the two labile bonds in the spacer chain. Second, a relatively simple MS/MS spectrum can be generated owing to favorable cleavage of labile bonds. And finally, the cross-linked peptide chains are dissociated from each other, and each then can be fragmented separately to get sequence information. Therefore, this novel type of cross-linker was named protein interaction reporter (PIR). To this end, two RINK groups were utilized to make our first-generation cross-linker using solid-phase peptide synthesis chemistry. The RINK group contains a bond more labile than peptide bonds during low-energy activation. The new cross-linker was applied to cross-link ribonuclease S (RNase S), a noncovalent complex of S-peptide and S-protein. The results demonstrated that the new cross-linker effectively reacted with RNase S to generate various types of cross-linked products. More importantly, the cross-linked peptides successfully released reporter ions during selective MS/MS conditions, and the dissociated peptide chains remained intact during MS(2), thus enabling MS(3) to be performed subsequently. In addition, dead-end, intra-, and inter-cross-linked peptides can be distinguished by analyzing MS/MS spectra.

Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions. Publishing Authors By Initials

X Tang,GR Munske,WF Siems,JE Bruce,

For similar enzymes and coenzymes: enzymes: hydrolases: esterases: ribonucleases research abstracts see: enzymes and coenzymes: enzymes: hydrolases: esterases: ribonucleases research

PUBMED ID PMID:

MEDLINE DATE:

Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Analytical chemistry

VOLUME: 77

Page Numbers: 311-8

Journal Abbreviation: Anal. Chem.

ISSN: 0003-2700

DAY: 1

MONTH: Jan

YEAR: 2005

Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370536

Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions. Keywords Mesh Terms:

KEYWORDS: Ribonucleases

MESH TERMS: chemistry

Chemical & Substance for Abstract: Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions. Information

Substance Name: ribonuclease S

Registry Number: EC 3.1.4.-

Grant and Affiliation Information for Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions.

AFFILIATION: Department of Chemistry, Washington State University, Pullman, WA 99164-4630, USA.

Country: United States

AGENCY: United States NCRR

GRANT: S10 RR 017805-01

ACRONYM: RR

MEDLINETA: Anal Chem

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