Lighting up Nobel Prize-winning studies with protein intrinsic disorder

Piersimoni, Lolita; Malek, Marina Abd el; Bhatia, Twinkle; Bender, Julian; Brankatschk, Christin; Sánchez, Jaime Calvo; Dayhoff, Guy W.; Ianni, Alessio Di; Parra, Jhonny Oscar Figueroa; Garcia-Martinez, Dailen; Hesselbarth, Julia; Köppen, Janett; Lauth, Luca M; Lippik, Laurin; Machner, Lisa; Sachan, Shubhra; Schmidt, L.D.; Selle, Robin; Skalidis, Ioannis; Sorokin, Oleksandr; Ubbiali, Daniele; Voigt, Bruno; Wedler, Alice; Wei, Alan An Jung; Zorn, Peter; Dunker, A. Keith; Köhn, Marcel; Sinz, Andrea; Uversky, Vladimir N.

doi:10.1007/s00018-022-04468-y

Cited by 7 publications

(2 citation statements)

References 259 publications

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“…Even though Volodya left Indiana in 2010, we continue to collaborate [ 42 , 43 ]. Words cannot express how much Volodya has helped me and our students over our many years together.…”

Section: The Impact Of Vladimir Uversky On the Scientific Community A...mentioning

confidence: 99%

Per Aspera ad Chaos: Vladimir Uversky’s Odyssey through the Strange World of Intrinsically Disordered Proteins

et al. 2023

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“…Even though Volodya left Indiana in 2010, we continue to collaborate [ 42 , 43 ]. Words cannot express how much Volodya has helped me and our students over our many years together.…”

Section: The Impact Of Vladimir Uversky On the Scientific Community A...mentioning

confidence: 99%

Per Aspera ad Chaos: Vladimir Uversky’s Odyssey through the Strange World of Intrinsically Disordered Proteins

et al. 2023

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“…It is one of the most studied and prominent representatives of intrinsically disordered proteins (IDPs) (5). The structural and functional characterization of IDPs has been recognized as a crucial task in structural biology, considering the abundance of proteins containing intrinsically disordered regions (IDRs) in all domains of life (archaea, bacteria, eukaryotes) and in viruses (6, 7). More than 40 years after the discovery of the prominent tumor suppressor protein the structure and spatial arrangement of the tetrameric p53 complex, remain elusive.…”

Section: Introductionmentioning

confidence: 99%

Structural Assessment of the Full-Length Wild-Type Tumor Suppressor Protein p53 by Mass Spectrometry-Guided Computational Modeling

Ianni

Tüting

Kipping

et al. 2022

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The tetrameric tumor suppressor p53 represents a great challenge for 3D-structural analysis due to its high degree of intrinsic disorder (ca. 40%). We aim to shed light on the structural and functional roles of p53's C-terminal region in full-length, wild-type human p53 tetramer and their importance for DNA binding. For this, we employed complementary techniques of structural mass spectrometry (MS) in an integrated approach with AI-based computational modeling. Our results show no major conformational differences in p53 between DNA-bound and DNA-free states, but reveal a substantial compaction of p53's C-terminal region. This supports the proposed mechanism of unspecific DNA binding to the C-terminal region of p53 prior to transcription initiation by specific DNA binding to the core domain of p53. The synergies between complementary structural MS techniques and computational modeling as pursued in our integrative approach is envisioned to serve as general strategy for studying intrinsically disordered proteins (IDPs) and intrinsically disordered region (IDRs).

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How protein fold: Insights from nuclear magnetic resonance spectroscopy

Zhuravelva

2024

Encyclopedia of Condensed Matter Physics

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Lighting up Nobel Prize-winning studies with protein intrinsic disorder

Cited by 7 publications

References 259 publications

Per Aspera ad Chaos: Vladimir Uversky’s Odyssey through the Strange World of Intrinsically Disordered Proteins

Per Aspera ad Chaos: Vladimir Uversky’s Odyssey through the Strange World of Intrinsically Disordered Proteins

Structural Assessment of the Full-Length Wild-Type Tumor Suppressor Protein p53 by Mass Spectrometry-Guided Computational Modeling

How protein fold: Insights from nuclear magnetic resonance spectroscopy

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