Multinuclear NMR and UV-Vis spectroscopy of site directed mutants of the diabetes drug target protein mitoNEET suggest that folding is intimately coupled to iron-sulfur cluster formation
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- 作者：S.K. Benson1 ; K.M. Boyce1 ; R.M. Bunker1 ; N.B. Collins1 ; K.J. Daily1 ; A.S. Esway1 ; G.T. Gilmore1 ; C.W. Hartzler1 ; G.P. Howard1 ; N.A. Kasmar1 ; K.J. Kennedy1 ; B.L. King1 ; T.N. Kordahi1 ; T.A. Mattioli1 ; D.M. Pugh1 ; L.A. Ray1 ; S.L. Ross1 ; M.H. Torcasio1 ; D.P. Webber1 ; D.L. Morris ; T.C. Leeper
- 关键词：MitoNEET ; Iron-sulfur cluster ; NMR ; UV-Vis ; Undergraduate research
- 刊名：Inorganic Chemistry Communications
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：63
- 期：Complete
- 页码：86-92
- 全文大小：1165 K
文摘
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MitoNEET's inorganic biochemistry was probed by site-directed mutagenesis.
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Iron–sulfur cluster stability was determined by NMR and UV/Vis.
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2Fe–2S cluster formation is coupled to domain folding.
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Authentic research in the classroom can be applied to answer biophysical questions.