Human islet amyloid polypeptide monomers form ordered [beta]-hairpins: a possible direct amyloidogenic precursor

Authors :: Dupuis, Nicholas F.
Chun Wu
Shea, Joan-Emma
Bowers, Michael T.
Source :: Journal of the American Chemical Society. Dec 30, 2009, Vol. 131 Issue 51, 18283-18292
Publication Year :: 2009
Abstract: The structural features of the human islet amyloid polypeptide (IAPP) monomer are probed by using a combination of ion mobility mass spectrometry (IMS-MS) and all-atom replica exchange molecular dynamics (REMD) simulations. The studies have provided evidence of a significant population of [beta]-hairpin conformers for the IAPP peptide.

Subjects :: Glycoproteins -- Structure
Glycoproteins -- Chemical properties
Islands of Langerhans -- Physiological aspects
Mass spectrometry -- Usage
Molecular dynamics -- Usage
Chemistry

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