Quantitative Protein Disorder Assessment Using NMR Chemical Shifts

Research output: Contribution to book/anthology/report/proceedingBook chapterResearchpeer-review

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.

Original languageEnglish
Title of host publicationIntrinsically Disordered Proteins
EditorsBirthe B. Kragelund, Karen Skriver
Number of pages15
Place of publicationNew York
PublisherHumana Press
Publication year2020
Pages303-317
ISBN (print)978-1-0716-0523-3
ISBN (Electronic)978-1-0716-0524-0
DOIs
Publication statusPublished - 2020
SeriesMethods in Molecular Biology
Volume2141
ISSN1064-3745

    Research areas

  • Chemical shift, CheZOD, Data interpretation, IDP, Intrinsically disordered proteins, NMR spectroscopy, POTENCI, Protein conformation, Software

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