By Katrine Kirkeby Skeby

This thesis deals readers a complete advent to amyloid proteins and the computational equipment used with them. Katrine Skeby significantly assesses and compares either the literature and the experiments played by way of different researchers, which additional elevates the standard and relevance of her personal paintings. Amyloid proteins are hugely advanced, and this study offers unprecedented insights, in particular in regards to the foundation of cytotoxicity and to constructing applied sciences for early detection, revealing intimately the molecular mechanisms at the back of hIAPP habit. a number of experiences in the thesis resolution tough questions which advertise destiny study into the houses of amyloid proteins.

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Additional resources for Computational Modelling of the Human Islet Amyloid Polypeptide

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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. Biochim Biophys Acta Biomembr 1808:2337–2342 119. Patil SM, Xu S, Sheftic SR, Alexandrescu AT (2009) Dynamic α-helix structure of micelle-bound human amylin.

The initial peptide structure was built with α-helical conformation, and was not an experimentally determined structure. They found that the Ser20Gly mutant adopts an L-shaped motif, which they speculate is the reason for the faster aggregation since it is structurally closer to the hairpin-like motif of hIAPP in the full amyloid fibril than an extended helical structure [149]. The all-atom simulation that is most similar to the common experimental conditions was performed by Jia et al. [153]. They simulated the process of binding of an hIAPP monomer to a POPG membrane bilayer with different initial orientations of the peptide above the membrane layer.

References 1. Branden C, Tooze J (1998) In Introduction to protein structure, 2nd edn. Garland 2. Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Ann Rev Biochem 75:333–366 3. Gorevic PD, Munoz PC, Casey TT, DiRaimondo CR, Stone WJ, Prelli FC, Rodrigues MM, Poulik MD, Frangione B (1986) Polymerization of intact β2-microglobulin in tissue causes amyloidosis in patients on chronic hemodialysis. Proc Natl Acad Sci USA 83:7908–7912 4. Virchow R (1854) Zur cellulose—frage.

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Computational Modelling of the Human Islet Amyloid by Katrine Kirkeby Skeby
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