Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form

Omar Davulcu, Xiaogang Niu, Lei Brüschweiler-Li, Rafael Brüschweiler, Jack J. Skalicky, Michael Chapman

Research output: Contribution to journalArticle

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Abstract

Nearly complete backbone resonance assignments for the 357 residue, 42 kDa enzyme arginine kinase in a transition state analogue (TSA) complex are presented. The TSA is a quaternary complex of arginine kinase, MgADP, arginine, and nitrate. About 93% (320 of 344) of the non-proline backbone amides were assigned using an enzyme enriched with (2)H, (13)C, and (15)N in combination with three enzyme samples prepared with a single (15)N-labeled amino acid (K, L, and R). The amide assignments will provide the foundation for investigating the dynamics of arginine kinase when in a TSA complex.

Original languageEnglish (US)
Pages (from-to)335-338
Number of pages4
JournalBiomolecular NMR Assignments
Volume8
Issue number2
DOIs
StatePublished - Oct 1 2014

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Arginine Kinase
Amides
Enzymes
Nitrates
Adenosine Diphosphate
Arginine
Amino Acids

ASJC Scopus subject areas

  • Medicine(all)

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Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form. / Davulcu, Omar; Niu, Xiaogang; Brüschweiler-Li, Lei; Brüschweiler, Rafael; Skalicky, Jack J.; Chapman, Michael.

In: Biomolecular NMR Assignments, Vol. 8, No. 2, 01.10.2014, p. 335-338.

Research output: Contribution to journalArticle

Davulcu, Omar ; Niu, Xiaogang ; Brüschweiler-Li, Lei ; Brüschweiler, Rafael ; Skalicky, Jack J. ; Chapman, Michael. / Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form. In: Biomolecular NMR Assignments. 2014 ; Vol. 8, No. 2. pp. 335-338.
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