Computational Modelling of the Human Islet Amyloid by Katrine Kirkeby Skeby

By Katrine Kirkeby Skeby

This thesis deals readers a accomplished creation to amyloid proteins and the computational tools used with them. Katrine Skeby seriously assesses and compares either the literature and the experiments played through different researchers, which extra elevates the standard and relevance of her personal paintings. Amyloid proteins are hugely advanced, and this learn offers remarkable insights, in particular in regards to the foundation of cytotoxicity and to constructing applied sciences for early detection, revealing intimately the molecular mechanisms in the back of hIAPP habit. a number of reviews in the thesis solution tough questions which advertise destiny study into the houses of amyloid proteins.

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Monticelli L, Kandasamy SK, Periole X, Larson RG, Tieleman DP, Marrink S-J (2008) The MARTINI coarse-grained force field: extension to proteins. J Chem Theory Comput 4:819–834 156. Xu W, Wei G, Su H, Nordenskiold L, Mu Y (2011) Effects of cholesterol on pore formation in lipid bilayers induced by human islet amyloid polypeptide fragments: a coarse-grained molecular dynamics study. Phys Rev E Stat Nonlinear Soft Matter Phys 84:051922 157. Periole X, Cavalli M, Marrink S-J, Ceruso MA (2009) Combining an elastic network with a coarse-grained molecular force field: structure, dynamics, and intermolecular recognition.

Jayasinghe S, Langen R (2005) Lipid membranes modulate the structure of islet amyloid polypeptide. Biochemistry 44:12113–12119 117. Nanga RPR, Brender JR, Xu J, Veglia G, Ramamoorthy A (2008) Structures of rat and human islet amyloid polypeptide IAPP1–19 in micelles by NMR spectroscopy. Biochemistry 47:12689–12697 118. Nanga RPR, Brender JR, Vivekanandan S, Ramamoorthy A (2011) Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment.

However, they are insoluble, making them difficult to study with traditional methods for structure determination, such as liquid-state NMR and X-ray crystallography. ss-NMR, however, has been successful in determining structural models for many amyloid fibrils. A combination of ss-NMR and restrained Langevin dynamics resulted in a model of an amyloid fibril formed by full-length hIAPP (Fig. 8) [22]. Fig. 8 ss-NMR structural model of hIAPP. a The two β-sheet layers are seen in blue and red. b The fibril seen from the end.

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