ArticleBiophysical journal2010
Conformational analysis of the partially disordered measles virus N(TAIL)-XD complex by SDSL EPR spectroscopy.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 60 citations in OpenAlex.
- Transient non-local interactions dominate the dynamics of measles virus NCommunications chemistry · 2025Article
- Vital for Viruses: Intrinsically Disordered Proteins.Journal of molecular biology · 2023Review
- NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins.Chemical reviews · 2022Review
- The Nucleocapsid of Paramyxoviruses: Structure and Function of an Encapsidated Template.Viruses · 2021Review
- Crowding Effects on the Structure and Dynamics of the Intrinsically Disordered Nuclear Chromatin Protein NUPR1.Frontiers in molecular biosciences · 2021Article
- How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication.Cellular and molecular life sciences : CMLS · 2017Review
- The structurally disordered paramyxovirus nucleocapsid protein tail domain is a regulator of the mRNA transcription gradient.Science advances · 2017Article
- Are Charge-State Distributions a Reliable Tool Describing Molecular Ensembles of Intrinsically Disordered Proteins by Native MS?Journal of the American Society for Mass Spectrometry · 2017Review
- Modulation of Re-initiation of Measles Virus Transcription at Intergenic Regions by PXD to NTAIL Binding Strength.PLoS pathogens · 2016Article
- Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment.International journal of molecular sciences · 2015Article
- Molecular basis for structural heterogeneity of an intrinsically disordered protein bound to a partner by combined ESI-IM-MS and modeling.Journal of the American Society for Mass Spectrometry · 2015Article
- Exploring intrinsically disordered proteins using site-directed spin labeling electron paramagnetic resonance spectroscopy.Frontiers in molecular biosciences · 2015Review
- Continuous wave W- and D-band EPR spectroscopy offer "sweet-spots" for characterizing conformational changes and dynamics in intrinsically disordered proteins.Biochemical and biophysical research communications · 2014Article
- Magnetic resonance access to transiently formed protein complexes.ChemistryOpen · 2014Article
- Multiscaled exploration of coupled folding and binding of an intrinsically disordered molecular recognition element in measles virus nucleoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Interaction between the C-terminal domains of measles virus nucleoprotein and phosphoprotein: a tight complex implying one binding site.Protein science : a publication of the Protein Society · 2012Article
- Plasticity in structural and functional interactions between the phosphoprotein and nucleoprotein of measles virus.The Journal of biological chemistry · 2012Article
- One-step generation of error-prone PCR libraries using Gateway® technology.Microbial cell factories · 2012Article
- Conformational selection underlies recognition of a molybdoenzyme by its dedicated chaperone.PloS one · 2012Article
- Expanding the proteome: disordered and alternatively folded proteins.Quarterly reviews of biophysics · 2011Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
To characterize the structure of dynamic protein systems, such as partly disordered protein complexes, we propose a novel approach that relies on a combination of site-directed spin-labeled electron paramagnetic resonance spectroscopy and modeling of local rotation conformational spaces. We applied this approach to the intrinsically disordered C-terminal domain of the measles virus nucleoprotein (N(TAIL)) both free and in complex with the X domain (XD, aa 459-507) of the viral phosphoprotein. By comparing measured and modeled temperature-dependent restrictions of the side-chain conformational spaces of 12 SL cysteine-substituted N(TAIL) variants, we showed that the 490-500 region of N(TAIL) is prestructured in the absence of the partner, and were able to quantitatively estimate, for the first time to our knowledge, the extent of the alpha-helical sampling of the free form. In addition, we showed that the 505-525 region of N(TAIL) conserves a significant degree of freedom even in the bound form. The latter two findings provide a mechanistic explanation for the reported rather high affinity of the N(TAIL)-XD binding reaction. Due to the nanosecond timescale of X-band EPR spectroscopy, we were also able to monitor the disordering in the 488-525 region of N(TAIL), in particular the unfolding of the alpha-helical region when the temperature was increased from 281 K to 310 K.
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