Abstract
Human serum albumin (HSA) is a versatile transport protein for various endogenous compounds and drugs. This study focuses on its highly relevant transport function for fatty acids in the circulatory system. While extensive crystallographic data on HSA–fatty acid binding exist, a new spectroscopic approach is used to gain information on the functional structure of HSA in solution. Using spin-labeled stearic acid and applying double electron–electron resonance (DEER) spectroscopy, the functional protein structure is accessed for the first time from the ligands’ point of view.
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Junk, M.J. (2012). The Functional Structure of Human Serum Albumin. In: Assessing the Functional Structure of Molecular Transporters by EPR Spectroscopy. Springer Theses. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-25135-1_3
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DOI: https://doi.org/10.1007/978-3-642-25135-1_3
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