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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.