Protein structure, Intrinsically disordered proteins, Crystallography, Protein folding and Measles Virus Nucleoprotein are her primary areas of study. Sonia Longhi works mostly in the field of Protein structure, limiting it down to topics relating to Protein domain and, in certain cases, Sequence, Functional studies and A protein, as a part of the same area of interest. Her Intrinsically disordered proteins research incorporates themes from Plasma protein binding, Computational biology and Circular dichroism.
Her Crystallography study also includes fields such as
Her main research concerns Phosphoprotein, Intrinsically disordered proteins, Crystallography, Virology and Protein structure. The various areas that Sonia Longhi examines in her Phosphoprotein study include Biophysics, Nucleoprotein and Henipavirus. Her Intrinsically disordered proteins study combines topics from a wide range of disciplines, such as Chemical physics, Plasma protein binding, Computational biology and Protein folding.
She works mostly in the field of Crystallography, limiting it down to concerns involving Intermolecular force and, occasionally, Crystal. Her Virology research integrates issues from RNA, Polymerase and Transcription. In her study, Sequence is inextricably linked to Protein domain, which falls within the broad field of Protein structure.
Her primary areas of investigation include Intrinsically disordered proteins, Phosphoprotein, Computational biology, Biophysics and Protein structure. The Intrinsically disordered proteins study which covers Protein folding that intersects with Peptide sequence and Chemical physics. Sonia Longhi undertakes interdisciplinary study in the fields of Phosphoprotein and Measles virus through her research.
Her work carried out in the field of Computational biology brings together such families of science as Proteome, Functional annotation and Artificial protein. Her biological study spans a wide range of topics, including Folding, Molecular recognition, Spin label and Protein secondary structure. Sonia Longhi has included themes like Protein tertiary structure, Coiled coil, Protein domain, Förster resonance energy transfer and Mass spectrometry in her Protein structure study.
Sonia Longhi focuses on Intrinsically disordered proteins, Phosphoprotein, Computational biology, Folding and Biophysics. Intrinsically disordered proteins is a subfield of Biochemistry that Sonia Longhi investigates. She performs multidisciplinary studies into Phosphoprotein and Measles virus in her work.
Her Computational biology research includes elements of Identification, Bioinformatics and Förster resonance energy transfer. The concepts of her Folding study are interwoven with issues in Functional annotation and Protein domain. Her Biophysics research is multidisciplinary, incorporating elements of Crystallography, Order, Plasma protein binding and Molecular recognition.
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Introducing Protein Intrinsic Disorder.
Johnny Habchi;Peter Tompa;Sonia Longhi;Vladimir N. Uversky.
Chemical Reviews (2014)
Assessing protein disorder and induced folding.
Véronique Receveur‐Bréchot;Jean‐Marie Bourhis;Vladimir N. Uversky;Vladimir N. Uversky;Bruno Canard.
Proteins (2005)
A Practical Overview of Protein Disorder Prediction Methods
François Ferron;Sonia Longhi;Bruno Canard;David Karlin.
Proteins (2006)
The C-terminal Domain of the Measles Virus Nucleoprotein Is Intrinsically Disordered and Folds upon Binding to the C-terminal Moiety of the Phosphoprotein
Sonia Longhi;Véronique Receveur-Bréchot;David Karlin;Kenth Johansson.
Journal of Biological Chemistry (2003)
DisProt 7.0: a major update of the database of disordered proteins.
Damiano Piovesan;Francesco Tabaro;Francesco Tabaro;Ivan Micetic;Marco Necci.
Nucleic Acids Research (2016)
Atomic resolution (1.0 Å) crystal structure of Fusarium solani cutinase: stereochemical analysis
Sonia Longhi;Mirjam Czjzek;Victor Lamzin;Anne Nicolas.
Journal of Molecular Biology (1997)
The severe acute respiratory syndrome-coronavirus replicative protein nsp9 is a single-stranded RNA-binding subunit unique in the RNA virus world
Marie Pierre Egloff;François Ferron;Valérie Campanacci;Sonia Longhi.
Proceedings of the National Academy of Sciences of the United States of America (2004)
Cytosolic 5′-Triphosphate Ended Viral Leader Transcript of Measles Virus as Activator of the RIG I-Mediated Interferon Response
Sébastien Plumet;Florence Herschke;Jean-Marie Bourhis;Hélène Valentin.
PLOS ONE (2007)
Exploring hydrophobic sites in proteins with xenon or krypton.
Thierry Prangé;Marc Schiltz;Lucile Pernot;Nathalie Colloc'h.
Proteins (1998)
What's in a name? Why these proteins are intrinsically disordered: Why these proteins are intrinsically disordered.
A Keith Dunker;M Madan Babu;Elisar Barbar;Martin Blackledge.
Intrinsically Disord Proteins , 1 (1) , Article e24157. (2013) (2013)
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