Paul Robustelli

Assistant Professor

Dartmouth College

United States

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Paul Robustelli is an Assistant Professor at Dartmouth College in the United States. His research focuses on intrinsically disordered proteins, exploring topics such as ensemble docking, folding-upon-binding pathways, and the molecular basis of small-molecule interactions. Recent publications include advancements in computational protein design and biophysical studies, contributing significantly to the understanding of protein dynamics and drug interactions.

Articles (13)

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2025

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2025

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2024

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2024

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2024

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2023

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2023

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2023

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2022

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2022

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2020

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2020

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2020

Collaborators (8)

Arthur G. Palmer

Columbia University

UNITED STATES

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M Bonomi

Université Paris Cité

FRANCE

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Tiago Cordeiro

Head of Laboratory (MOSTMICRO-ITQB)

Universidade Nova de Lisboa Instituto de Tecnologia Química e Biológica

PORTUGAL

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Sylvie RICARD-BLUM

Professor

Université Claude Bernard Lyon 1

FRANCE

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Xavier Salvatella

Research Professor

ICREA

SPAIN

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Peter Tompa

Vrije Universiteit Brussel

BELGIUM

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Tâp Ha-Duong

Université Paris-Saclay

FRANCE

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Mateusz Biesaga

Head of Technology

SPAIN

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Paul Robustelli

Research Interests

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About

Articles (13)

Ensemble Docking for Intrinsically Disordered Proteins

Covalent Adducts Formed by the Androgen Receptor Transactivation Domain and Small Molecule Drugs Remain Disordered

Extending computational protein design to intrinsically disordered proteins

Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model

Dissecting the biophysics and biology of intrinsically disordered proteins

Clustering Heterogeneous Conformational Ensembles of Intrinsically Disordered Proteins with t-Distributed Stochastic Neighbor Embedding

PED in 2024: improving the community deposition of structural ensembles for intrinsically disordered proteins

Rational optimization of a transcription factor activation domain inhibitor

Small molecules targeting the disordered transactivation domain of the androgen receptor induce the formation of collapsed helical states

Molecular Basis of Small-Molecule Binding to α-Synuclein

Quantifying the Relationship between Conformational Dynamics and Enzymatic Activity in Ribonuclease HI Homologues

Mechanism of Coupled Folding-upon-Binding of an Intrinsically Disordered Protein

Development of a Force Field for the Simulation of Single-Chain Proteins and Protein–Protein Complexes

Collaborators (8)

Arthur G. Palmer

M Bonomi

Tiago Cordeiro

Sylvie RICARD-BLUM

Xavier Salvatella

Peter Tompa

Tâp Ha-Duong

Mateusz Biesaga

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