Dimerization interface and dynamic properties of yeast IF1 revealed by Site-Directed Spin Labeling EPR spectroscopy
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- 作者：Nolwenn Le Bretona ; 1 ; Tiona Adrianaivomananjaonab ; c ; d ; 1 ; Guillaume Gerbauda ; Emilien Etiennea ; Elena Bisettoc ; e ; Alain Dautantf ; Bruno Guigliarellia ; Francis Harauxc ; d ; francis.haraux@cea.fr" class="auth_mail" title="E-mail the corresponding author ; Marlè ; ne Martinhoa ; Valé ; rie Bellea ; belle@imm.cnrs.fr" class="auth_mail" title="E-mail the corresponding author
- 关键词：CD ; Circular Dichroism ; cw ; continuous wave ; DEER ; Double Electron&ndash ; Electron Resonance ; DTT ; dithiothreitol ; EPR ; Electron Paramagnetic Resonance ; IF1 ; endogenous inhibitory peptide of mitochondrial ATP synthase ; bIF1 ; IF1 from bovine ; yIF1 ; IF1 from yeast ; MMM ; Multiscale Modeling of Macromolecules ; MTSL ; 1-oxyl-2 ; 2 ; 5 ; 5-tetramethyl-δ3-pyrroline-3-methyl methanethiosulfonate ; rt ; room temperature ; SDSL ; Site-Directed Spin Labeling ; wt ; wild type ; TFE ; trifluoroethanol
- 刊名：Biochimica et Biophysica Acta (BBA) - Bioenergetics
- 出版年：2016
- 出版时间：January 2016
- 年：2016
- 卷：1857
- 期：1
- 页码：89-97
- 全文大小：1020 K
文摘
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Yeast IF1 dimerizes through its central part.
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Yeast IF1 dimer is non-inhibitory.
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The C-terminal region of yeast IF1 is disordered.
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A conformational change is driven by pH variation.