期刊
BIOPHYSICAL CHEMISTRY
卷 151, 期 3, 页码 187-189出版社
ELSEVIER
DOI: 10.1016/j.bpc.2010.06.005
关键词
Protein-protein interaction; Lactoferrin; Self-assembly; Stereospecific
Gathering experimental evidence suggests that bovine as well as human lactoferrin self-associate in aqueous solution. Still, a molecular level explanation is unavailable. Using force field based molecular modeling of the protein-protein interaction free energy we demonstrate (1) that lactoferrin forms highly stereo-specific dimers at neutral pH and (2) that the self-association is driven by a high charge complementarity across the contact surface of the proteins. Our theoretical predictions of dimer formation are verified by electrophoretic mobility and N-terminal sequence analysis on bovine lactoferrin. (C) 2010 Elsevier B.V. All rights reserved.
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