Peter Agback

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

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

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.

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

This study demonstrates that a tailored titanium dioxide nanoparticle specifically recognizes a unique site on the full-length SARS-CoV-2 nsp1 protein, suggesting potential for targeted viral intervention.

This paper reports the NMR resonance assignment and structural analysis of SARS-CoV-2 nsp1 protein and its mutants, revealing unique secondary structure features and dynamic behavior.