Dmitry M. Lesovoy

Insight into Malt1 activation mechanism through synergetic approach of AlphaFold, MD Simulation and NMR dynamic analyses

The paper investigates MALT1 activation dynamics using a combination of AlphaFold, MD simulations, and NMR analyses, revealing how ionic strength influences its conformational states.

Accurate Protein Dynamic Conformational Ensembles: Combining AlphaFold, MD and Amide 15N(1H) NMR Relaxation.

The paper combines AlphaFold, MD simulations, and NMR relaxation data to identify biologically relevant protein conformational ensembles for a specific bacterial protein.

Crystallographic and NMR studies of Streptococcus pneumonia LCP protein PsrSp indicate the importance of dynamics in four long loops for ligand specificity

The paper determines the crystal structure of PsrSp and uses NMR to analyze its dynamics, showing that four long loops contribute to ligand specificity through their mobility.

Towards understanding of allostery in MALT1: a possible role of interdomain motions as revealed by NMR and AlphaFold

The paper investigates the dynamic behavior of MALT1 using NMR and AlphaFold to reveal interdomain motions involved in allosteric regulation.