Abstract
Disorder is vital for the biological function of many proteins. The huge diversity found in disorder composition and amplitude reflects the complexity and pluripotency of intrinsically disordered proteins (IDPs). The first step toward a better understanding of IDPs is a quantitative and position-specific experimental characterization, and nuclear magnetic resonance (NMR) spectroscopy has emerged as the method of first choice. Here, we describe how to quantitatively assess the local balance between order and disorder in proteins by utilizing the Chemical shift Z-score for assessing Order/Disorder (CheZOD Z-score). This order/disorder metric is computed from the difference between experimentally determined NMR chemical shifts and computed random coil reference values. We explain in detail how CheZOD Z-scores are calculated fast and easily, either by using a python executable or by data submission to a server.
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Acknowledgments
We are indebted to all researchers who have deposited NMR data in the BMRB and are grateful to the visionaries who have initiated this data collection initiative. Ian H. Gotliebsen is acknowledged for technical support.
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Nielsen, J.T., Mulder, F.A.A. (2020). Quantitative Protein Disorder Assessment Using NMR Chemical Shifts. In: Kragelund, B.B., Skriver, K. (eds) Intrinsically Disordered Proteins. Methods in Molecular Biology, vol 2141. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0524-0_15
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DOI: https://doi.org/10.1007/978-1-0716-0524-0_15
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