Sandro Bottaro

This paper introduces OPES multithermal sampling to efficiently explore rare conformations in intrinsically disordered proteins, revealing transient tertiary structures in ACTR.

The paper introduces a benchmark for evaluating protein ensemble generators across ordered and disordered proteins and presents a new model that improves performance on disordered regions.

This study identifies acidic patches in the MYC N-terminal disordered domain essential for oncogenesis and chromatin interaction, offering new therapeutic targets.

The paper improves protein stability prediction by modifying existing models with a self-derived term, enhancing their performance without additional training or data.

Barnaba is a Python library for analyzing nucleic acids structures and molecular trajectories, offering tools for distance calculation, cluster analysis, motif search, and elastic network modeling.

This paper introduces a Bayesian/Maximum Entropy method to refine molecular simulations using experimental data, producing a conformational ensemble that matches experimental values while maximizing entropy.