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Evidence against a Permanently Folded Nucleation Sequence in the Intrinsically Disordered Protein Stathmin Measured by Site-Directed Spin Labeling EPR Spectroscopy

机译：针对定点自旋标记EPR光谱测量固有紊乱蛋白Stathmin中永久折叠成核序列的证据。

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Foltz Gretchen; Doupey Tonia G.; Kamel Joseph G.; Bridges Michael D.;
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2. Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy. [J] . Belle V, Rouger S, Costanzo S, Proteins: Structure, Function, and Genetics . 2008,第4期

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3. Multiple Structural States Exist Throughout the Helical Nucleation Sequence of the Intrinsically Disordered Protein Stathmin, As Reported by Electron Paramagnetic Resonance Spectroscopy [J] . Chui Ashley J., Lopez Carlos J., Brooks Evan K., Biochemistry . 2015,第9期

机译：如电子顺磁共振波谱报告的那样，在固有的无序蛋白Stathmin的螺旋成核序列中存在多个结构状态。
4. Pulsed EPR Distance Measurements on Spin-Labeled Proteins and Protein Complexes: Opportunities and Limitations [C] . Gunnar Jeschke, Aleksei Volkov, Yevhen Polyhach Asia-Pacific EPR/ESR Symposium . 2006

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5. Genome-wide prediction of intrinsic disorder; sequence alignment of intrinsically disordered proteins [D] . Midic, Uros 2012

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6. Exploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy [O] . Nolwenn Le Breton, Marlène Martinho, Elisabetta Mileo, 2015

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Evidence against a Permanently Folded Nucleation Sequence in the Intrinsically Disordered Protein Stathmin Measured by Site-Directed Spin Labeling EPR Spectroscopy

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