The Characterization of Weak Protein–Protein Interactions: Evidence from DEER for the Trimerization of a von Willebrand Factor A Domain in Solution | Zendy

Banham Janet E. | Zendy; Timmel Christiane R. | Zendy; Abbott Rachel J. M. | Zendy; Lea Susan M. | Zendy; Jeschke Gunnar | Zendy

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The Characterization of Weak Protein–Protein Interactions: Evidence from DEER for the Trimerization of a von Willebrand Factor A Domain in Solution

Author(s) -

Banham Janet E.,

Timmel Christiane R.,

Abbott Rachel J. M.,

Lea Susan M.,

Jeschke Gunnar

Publication year - 2006

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200503720

Subject(s) - von willebrand factor , macromolecule , nitroxide mediated radical polymerization , domain (mathematical analysis) , chemistry , characterization (materials science) , electron paramagnetic resonance , crystallography , biophysics , nanotechnology , materials science , nuclear magnetic resonance , biochemistry , polymer , physics , biology , copolymer , mathematics , organic chemistry , mathematical analysis , platelet , radical polymerization , immunology

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.

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