TY - JOUR
T1 - Approaching Protein Aggregation and Structural Dynamics by Equilibrium and Nonequilibrium Paramagnetic Perturbation
AU - Hunashal, Yamanappa
AU - Percipalle, Mathias
AU - Molnár, Tamás
AU - Kardos, Jòzsef
AU - Percipalle, Piergiorgio
AU - Esposito, Gennaro
N1 - Publisher Copyright:
© 2022 American Chemical Society. All rights reserved.
PY - 2022/8/9
Y1 - 2022/8/9
N2 - 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.
AB - 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.
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U2 - 10.1021/acs.analchem.2c00751
DO - 10.1021/acs.analchem.2c00751
M3 - Article
AN - SCOPUS:85135894637
SN - 0003-2700
VL - 94
SP - 10949
EP - 10958
JO - Analytical Chemistry
JF - Analytical Chemistry
IS - 31
ER -