R. Crehuet

Checkpoint activation by Spd1: a competition-based system relying on tandem disordered PCNA binding motifs

The paper identifies a PIP-box motif in Spd1 that competes with another PCNA binding site to regulate checkpoint activation in yeast.

A glutamine-based single α-helix scaffold to target globular proteins

This paper introduces a method to design peptides that fold into single α-helices using glutamine side chain to main chain hydrogen bonds, enabling targeted interactions with globular proteins.

Mg2+-dependent conformational equilibria in CorA: an integrated view on transport regulation

This study investigates the conformational dynamics of CorA, revealing Mg2+-dependent conformational equilibria and dynamic behavior through SANS, MD simulations, and NMR.

Accurate model of liquid-liquid phase behaviour of intrinsically-disordered proteins from data-driven optimization of single-chain properties

The paper develops a coarse-grained model of intrinsically disordered proteins using data-driven optimization to accurately predict phase behaviour and self-association.

DEER-PREdict: Software for Efficient Calculation of Spin-Labeling EPR and NMR Data from Conformational Ensembles

DEER-PREdict calculates EPR and NMR data from protein conformational ensembles to validate models and interpret experiments.

Bayesian-Maximum-Entropy reweighting of IDPs ensembles based on NMR chemical shifts

The paper introduces a Bayesian-Maximum-Entropy method to reweight IDP ensembles using NMR chemical shifts, showing it provides consistent results even when other fitting assessment methods fail.

Analyzing and comparing the radius of gyration and hydrodynamic radius in conformational ensembles of intrinsically disordered proteins

The paper calculates radius of gyration and hydrodynamic radius from computationally generated conformational ensembles of intrinsically disordered proteins and integrates SAXS and NMR data using Bayesian/Maximum Entropy methods.

Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in the activation domain of a transcription factor

This study investigates how polyglutamine tract length affects the structure and function of the androgen receptor, revealing hydrogen bonds that stabilize a helical conformation linked to transcriptional activity and disease.