Chemical shift perturbation analysis: Structural basis of client specificity in mitochondrial membrane-protein chaperones
Published: 30 May 2020| Version 1 | DOI: 10.17632/8cr8rvtddm.1
Contributors:
Iva Sučec, Paul SchandaDescription
NMR analysis of TIM8.13 and TIM9.10, chaperones of the mitochondrial inner-membrane space (IMS), upon addition of either full-length Tim23, IMS domain fragment of Tim23 or cyclic VDAC(257-279) peptide. Residue-wise CSP are calculated as the weighted sum of 1H and 15N chemical shifts and additionally as weighted sum of 1H and 13C chemical shifts for TIM9.10 interaction with the full-length Tim23. Changes in Tim23 peak intensities upon addition of chaperone are calculated as the ratios of the peak volume in the complex over the apo-Tim23(IMS).
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Categories
Structural Biology, Nuclear Magnetic Resonance, Chaperone Protein, Mitochondrion