Publications

NMR methodology using extreme Carr-Purcell-Meiboom-Gill (eCPMG) experiments to characterize protein dynamics at sub-millisecond timescales. The technique allows investigation of rapid conformational changes in proteins.

The work includes:

• Development and application of eCPMG relaxation dispersion experiments
• Detection of fast protein dynamics at sub-millisecond timescales
• Methodology for studying conformational exchange processes
• Applications to structure-function relationships in biomolecules

The method provides tools to probe rapid protein dynamics and understand how proteins function through conformational changes.

Solution structure of the human PALB2 coiled-coil domain determined using NMR spectroscopy. The domain forms an antiparallel homodimer. We investigated how missense mutations affect the protein’s fold, interactions, and functional efficiency in homologous recombination.

Key findings:

• Solution structure of PALB2 coiled-coil domain reveals an antiparallel homodimer
• Analysis of clinically relevant missense mutations and their structural impact
• Correlation between structural disruption and homologous recombination efficiency
• Approach for evaluating variants of uncertain significance in genetic counseling

PALB2 connects BRCA proteins at DNA damage sites, playing a role in DNA damage repair.