Approaching Protein Aggregation and Structural Dynamics by Equilibrium and Nonequilibrium Paramagnetic Perturbation

Yamanappa Hunashal, Mathias Percipalle, Tamás Molnár, Jòzsef Kardos, Piergiorgio Percipalle, Gennaro Esposito

Research output: Contribution to journalArticlepeer-review

Abstract

PENELOP (Paramagnetic Equilibrium vs Nonequilibrium magnetization Enhancement or LOss Perturbation) is the presented nuclear magnetic resonance (NMR) approach to identify at once the location of proteins' exposed surface, hindered accessibility, and exchange processes occurring on a μs-ms time scale. In addition to mapping the protein surface accessibility, the application of this method under specific conditions makes it possible to distinguish conformational mobility and chemical exchange processes, thereby providing an alternative to characterization by more demanding techniques (transverse relaxation dispersion, saturation transfer, and high-pressure NMR). Moreover, its high sensitivity enables studying samples at low, physiologically more relevant concentrations. Association, dynamics, and oligomerization are addressed by PENELOP for a component of SARS-CoV-2 replication transcription complex and an amyloidogenic protein.

Original languageEnglish (US)
Pages (from-to)10949-10958
Number of pages10
JournalAnalytical Chemistry
Volume94
Issue number31
DOIs
StatePublished - Aug 9 2022

ASJC Scopus subject areas

  • Analytical Chemistry

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