Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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

Authors:	Omar Davulcu Xiaogang Niu Lei Brüschweiler-Li Rafael Brüschweiler Jack J Skalicky Michael S Chapman

Institution:	1. Department of Biochemistry and Molecular Biology, Oregon Health and Science University, 3181 S.W. Sam Jackson Park Road, Portland, OR, 97239-3098, USA 2. Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, 32306, USA 3. Department of Biochemistry, University of Utah, Salt Lake City, UT, 84112-5650, USA

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 ²H, ¹³C, and ¹⁵N in combination with three enzyme samples prepared with a single ¹⁵N-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.

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