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Hocking, H.G. ; Zangger, K.* ; Madl, T.

Studying the structure and dynamics of biomolecules by using soluble paramagnetic probes.

ChemPhysChem 14, 3082-3094 (2013)
Verlagsversion Volltext DOI PMC
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
Characterisation of the structure and dynamics of large biomolecules and biomolecular complexes by NMR spectroscopy is hampered by increasing overlap and severe broadening of NMR signals. As a consequence, the number of available NMR spectroscopy data is often sparse and new approaches to provide complementary NMR spectroscopy data are needed. Paramagnetic relaxation enhancements (PREs) obtained from inert and soluble paramagnetic probes (solvent PREs) provide detailed quantitative information about the solvent accessibility of NMR-active nuclei. Solvent PREs can be easily measured without modification of the biomolecule; are sensitive to molecular structure and dynamics; and are therefore becoming increasingly powerful for the study of biomolecules, such as proteins, nucleic acids, ligands and their complexes in solution. In this Minireview, we give an overview of the available solvent PRE probes and discuss their applications for structural and dynamic characterisation of biomolecules and biomolecular complexes.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Korrespondenzautor
Schlagwörter Magnetic Properties ; Nmr Spectroscopy ; Proteins ; Solvent Effects ; Structural Biology; Probing Protein-structure ; Proton-magnetic-resonance ; Lanthanide-induced Shifts ; Micelle-bound Peptides ; Surface Accessibility ; Nmr-spectra ; Relaxation Enhancements ; Solvent Perturbation ; Immersion Depth ; Spin Relaxation
ISSN (print) / ISBN 1439-4235
e-ISSN 1439-7641
Zeitschrift ChemPhysChem
Quellenangaben Band: 14, Heft: 13, Seiten: 3082-3094 Artikelnummer: , Supplement: ,
Verlag Wiley
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Structural Biology (STB)