Isabella Felli

Associate Professor

University of Arkansas - Rome Center

Italy

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About

Isabella Felli is an Associate Professor at the University of Arkansas - Rome Center in Italy. Her research areas include the study of protein interactions and conformational dynamics, particularly in relation to SARS-CoV-2 nucleocapsid protein and intrinsically disordered proteins, utilizing advanced NMR spectroscopy techniques. Recent publications reflect her focus on structural and dynamic complexity in biological systems.

Articles (18)

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2025

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2020

Collaborators (6)

Guido Pintacuda

Université Claude Bernard Lyon 1

FRANCE

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Simone Kosol

Lecturer (Biochemistry)

Medical School Berlin

GERMANY

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Maria Grazia Murrali

UCLA Division of Physical Sciences

UNITED STATES

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Roberta Pierattelli

Full Professor

Università degli Studi di Napoli Federico II

ITALY

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Michael Assfalg

Associate Professor

University of Verona

ITALY

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Alessandro Piai

Senior Research Investigator, Head of NMR

IRBM Science Park

ITALY

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Isabella Felli

Research Interests

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About

Articles (18)

Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain

Exploring the Role of Structural and Dynamic Complexity in SARS-CoV-2 Nucleocapsid Protein–Heparin Interactions by NMR

Revealing the Potential of a Chimaera: a Peptide‐Peptide Nucleic Acid Molecule Designed To Interact with the SARS‐CoV‐2 Nucleocapsid Protein

Revealing the Potential of a Chimaera: a Peptide‐Peptide Nucleic Acid Molecule Designed To Interact with the SARS‐CoV‐2 Nucleocapsid Protein

Are Protein Conformational Ensembles in Agreement with Experimental Data? A Geometrical Interpretation of the Problem

Intrinsically disordered proteins studied by NMR spectroscopy

Optimal 13C NMR investigation of intrinsically disordered proteins at 1.2 GHz

Disentangling the Complexity in Protein Complexes Using Complementary Isotope-Labeling and Multiple-Receiver NMR Spectroscopy

13C Direct Detected NMR for Challenging Systems

Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues

The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR

Multimodal Response to Copper Binding in Superoxide Dismutase Dynamics

Frontispiece: Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments

Frontispiz: Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments

Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments

Monitoring the Interaction of α‐Synuclein with Calcium Ions through Exclusively Heteronuclear Nuclear Magnetic Resonance Experiments

Picometer Resolution Structure of the Coordination Sphere in the Metal-Binding Site in a Metalloprotein by NMR

Interaction between the scaffold proteins CBP by IQGAP1 provides an interface between gene expression and cytoskeletal activity

Collaborators (6)

Guido Pintacuda

Simone Kosol

Maria Grazia Murrali

Roberta Pierattelli

Michael Assfalg

Alessandro Piai

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