Cited by 1.1k
University of Oxford
Publishes on Electron Spin Resonance Studies, Lanthanide and Transition Metal Complexes, Magnetism in coordination complexes. 7 papers and 1.3k citations.
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Distance determination: A double electron electron resonance (DEER) measurement of a distance of 6.1 nm (green lines) between singly nitroxide-labeled human von Willebrand Factor A domains demonstrates oligomerization of this domain in dilute solution (see structure); probably in an arrangement similar to that observed in the crystal structure. The DEER technique should be generally applicable for characterizing noncovalent interactions between macromolecules in solution.
Human oxy-hemoglobin was spin labelled at the two -93 cysteine positions with three different spin labels. Continuous wave electron paramagnetic resonance (CW EPR) was used to assess the dynamics of the attached spin labels in solution at room temperature. Solutions were frozen to 50 K and the distance between the spin labels was measured using the double electron electron resonance (DEER) pulsed EPR technique. The two sets of results were compared to the crystal structure of the protein and were found to be consistent with a model where the spin labels tend to adopt a less rigid surface exposed conformation in solution, but are positioned in a protein pocket in the frozen state.
Abstandsmessung: Die Doppel-Elektronen-Elektronen-Resonanz(DEER)-Messung eines Abstands von 6.15 nm in nitroxidmarkierter menschlicher Von-Willebrand-Faktor-A-Domäne (siehe Bild) belegt die Oligomerisierung dieser Domäne in verdünnter Lösung, wahrscheinlich in einer ähnlichen Molekülanordnung wie in der Kristallstruktur. DEER sollte allgemein für die Charakterisierung nichtkovalenter Wechselwirkungen zwischen Makromolekülen in Lösung anwendbar sein.