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Approaching Protein Aggregation and Structural Dynamics by Equilibrium and Nonequilibrium Paramagnetic Perturbation.
Hunashal, Yamanappa; Percipalle, Mathias; Molnár, Tamás; Kardos, Jòzsef; Percipalle, Piergiorgio; Esposito, Gennaro.
  • Hunashal Y; Chemistry Program, Science Division, New York University Abu Dhabi, Abu Dhabi 129188, United Arab Emirates.
  • Percipalle M; Dipartimento di Area Medica, Universita' di Udine, P.le Kolbe 4, 33100 Udine, Italy.
  • Molnár T; Chemistry Program, Science Division, New York University Abu Dhabi, Abu Dhabi 129188, United Arab Emirates.
  • Kardos J; Department of Chemistry and Magnetic Resonance Center, University of Florence, 50019 Florence, Italy.
  • Percipalle P; ELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest 1117, Hungary.
  • Esposito G; ELTE NAP Neuroimmunology Research Group, Department of Biochemistry, Eötvös Loránd University, Budapest 1117, Hungary.
Anal Chem ; 94(31): 10949-10958, 2022 08 09.
Article in English | MEDLINE | ID: covidwho-1960210
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Protein Aggregates / COVID-19 Limits: Humans Language: English Journal: Anal Chem Year: 2022 Document Type: Article Affiliation country: Acs.analchem.2c00751

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Protein Aggregates / COVID-19 Limits: Humans Language: English Journal: Anal Chem Year: 2022 Document Type: Article Affiliation country: Acs.analchem.2c00751