AFM Imaging Reveals Topographic Diversity of Wild Type and Z Variant Polymers of Human α1-Proteinase Inhibitor

α1-Proteinase inhibitor (antitrypsin) is a canonical example of the serpin family member that binds and inhibits serine proteases. The natural metastability of serpins is crucial to carry out structural rearrangements necessary for biological activity. However, the enhanced metastability of the muta...

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Veröffentlicht in:	PloS one 2016-03, Vol.11 (3), p.e0151902-e0151902
Hauptverfasser:	Gaczynska, Maria, Karpowicz, Przemyslaw, Stuart, Christine E, Norton, Malgorzata G, Teckman, Jeffrey H, Marszal, Ewa, Osmulski, Pawel A
Format:	Artikel
Sprache:	eng
Schlagworte:	60 APPLIED LIFE SCIENCES Addition polymerization alpha 1-Antitrypsin - chemistry Animal models Atomic force microscopy Atomic structure Biological activity Biopolymers - chemistry Computer simulation Crystal structure Disease Earth Sciences Etiology Guanidine Guanidine hydrochloride Heat treatment Humans Inhibitors Liver Medicine Metastable state Microscopy Microscopy, Atomic Force - methods Monomers Mutation Oligomers Periodic variations Periodicity pH effects Physical Sciences Polymerization Polymers Proteinase Research and Analysis Methods Serine Serine proteinase inhibitors Serpins Topography Transgenic mice
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