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Updated: Mar 7, 2026

Author Spotlight: Exploring Intrinsically Disordered Protein Dynamics Through NMR Relaxation Experiments
Published on: November 1, 2024
Deciphering the mechanisms of binding induced folding at nearly atomic resolution: The Φ value analysis applied to
Stefano Gianni1, Jakob Dogan2, Per Jemth2
1Dipartimento di Scienze Biochimiche "A. Rossi Fanelli"; Istituto di Biologia e Patologia Molecolari del CNR; Università di Roma "La Spaienza"; Rome, Italy; Department of Chemistry; University of Cambridge; Cambridge, UK.
Abstract:
The Φ value analysis is a method to analyze the structure of metastable states in reaction pathways. Such a methodology is based on the quantitative analysis of the effect of point mutations on the kinetics and thermodynamics of the probed reaction. The Φ value analysis is routinely used in protein folding studies and is potentially an extremely powerful tool to analyze the mechanism of binding induced folding of intrinsically disordered proteins. In this review we recapitulate the key equations and experimental advices to perform the Φ value analysis in the perspective of the possible caveats arising in intrinsically disordered systems. Finally, we briefly discuss some few examples already available in the literature.
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