AI Article Synopsis
- The study used electron spin resonance (ESR) to examine the binding of a specific fatty acid to serum albumin at various temperatures.
- Researchers identified two types of fatty acid behavior: one where the molecules are strongly immobilized and another where they are weakly immobilized.
- The findings revealed that under normal physiological conditions, fatty acid molecules continuously move between specific binding sites and other spaces within the albumin protein structure.
Article Abstract
Conventional ESR spectra of 16-doxyl-stearic acid bound to bovine and human serum albumin were recorded at different temperatures in order to investigate the status of spin-labeled fatty acid in the interior of the protein globule. A computer spectrum simulation of measured spectra, performed by non-linear least-squares fits, clearly showed two components corresponding to strongly and weakly immobilized fatty acid molecules. The two-component model was verified on spectra measured at different pH. Thermodynamic parameters of the spin probe exchange between two spin probe states were analyzed. It was concluded that at physiological conditions, fatty acid molecules permanently migrate in the globule interior between the specific binding sites and a space among albumin domains.
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| http://dx.doi.org/10.1016/j.bbrc.2007.06.140 | DOI Listing |
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