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The Distribution of Fatty Acids Reveals the Functional Structure of Human Serum Albumin
Author(s) -
Junk Matthias J. N.,
Spiess Hans Wolfgang,
Hinderberger Dariush
Publication year - 2010
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.201003495
Subject(s) - human serum albumin , chemistry , albumin , flexibility (engineering) , site directed spin labeling , electron paramagnetic resonance , biochemistry , biophysics , biology , nuclear magnetic resonance , physics , mathematics , statistics , membrane
Flexible on the outside : The functional structure of the transport protein in human blood, human serum albumin (HSA), was characterized by distance measurements with double electron–electron resonance (DEER) spectroscopy on spin‐labeled fatty acids that are bound to HSA. The functional protein structure derived has a more rigid inner core, while the surface of the protein shows much greater structural flexibility.