The Functional Structure of Human Serum Albumin

Chapter
Part of the Springer Theses book series (Springer Theses)

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.

Keywords

Electron Paramagnetic Resonance Human Serum Albumin Electron Paramagnetic Resonance Spectrum Pump Pulse Modulation Depth 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 2012

Authors and Affiliations

  1. 1.Max Planck Institute for Polymer ResearchMainzGermany

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