On the molecular structure of human neuroserpin polymers
Proteins: Structure, Function and Bioinformatics, ISSN: 0887-3585, Vol: 80, Issue: 1, Page: 8-13
2012
- 11Citations
- 29Captures
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Metrics Details
- Citations11
- Citation Indexes11
- CrossRef11
- 11
- Captures29
- Readers29
- 29
Article Description
The polymerization of serpins is at the root of a large class of diseases; the molecular structure of serpin polymers has been recently debated. In this work, we study the polymerization kinetics of human neuroserpin by Fourier Transform Infra Red spectroscopy and by time-lapse Size Exclusion Chromatography. First, we show that two distinct neuroserpin polymers, formed at 45 and 85°C, display the same isosbestic points in the Amide I′ band, and therefore share common secondary structure features. We also find a concentration independent polymerization rate at 45°C suggesting that the polymerization rate-limiting step is the formation of an activated monomeric species. The polymer structures are consistent with a model that predicts the bare insertion of portions of the reactive center loop into the A β-sheet of neighboring serpin molecule, although with different extents at 45 and 85°C. © 2011 Wiley Periodicals, Inc.
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