The Distribution of Fatty Acids Reveals the Functional Structure of Human Serum Albumin

被引：66

作者：

Junk, Matthias J. N. ^{[1
]}

Spiess, Hans Wolfgang ^{[1
]}

Hinderberger, Dariush ^{[1
]}

机构：

[1] Max Planck Inst Polymer Res, D-55128 Mainz, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2010年 / 49卷 / 46期

关键词：

albumin; EPR spectroscopy; fatty acids; nanostructures; protein structures; BINDING-SITES; EPR SPECTROSCOPY; PULSE EPR; BOVINE; PROTEINS; DISTANCES; UBIQUITIN; PELDOR;

D O I：

10.1002/anie.201003495

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

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 electronelectron 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. © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：8755 / 8759

页数：5

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