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Lipids in Protein Misfolding by Olga Gursky

By Olga Gursky

​Protein conversion from a water-soluble local conformation to the insoluble aggregates and fibrils, that may deposit in amyloid plaques, underlies greater than 20 human ailments, representing a huge public ailment and a systematic problem. this sort of conversion is named protein misfolding. Protein misfolding may also contain error within the topology of the folded proteins and their meeting in lipid membranes. Lipids are present in approximately all amyloid deposits in vivo, and will severely effect protein misfolding in vitro and in vivo in lots of other ways. This publication specializes in fresh advances in our knowing of the position of lipids in modulating the misfolding of varied proteins. the most emphasis is at the simple biophysical reviews that handle molecular foundation of protein misfolding and amyloid formation, and the position of lipids during this advanced process.

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Annu Rev Genet 43:67–93 Hessa T, Kim H, Bihlmaier K, Lundin C, Boekel J, Andersson H, Nilsson I, White SH, Von Heijne G (2005) Recognition of transmembrane helices by the endoplasmic reticulum translocon. Nature 433(7024):377–381 Hessa T, Meindl-Beinker NM, Bernsel A, Kim H, Sato Y, Lerch-Bader M, Nilsson I, White SH, Von Heijne G (2007) Molecular code for transmembrane-helix recognition by the Sec61 translocon. Nature 450(7172):1026–1030 Hite RK, Li Z, Walz T (2010) Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals.

2002). Thus, the protein stability enhancement by PEs originates from the nonspecific physical properties of the bilayer rather than from the specific head group interactions. Lipid-dependence of the thermodynamic stability of polytopic TM α-helical membrane proteins has not been studied yet in a lipid bilayer. However, the influence of lipid composition on the stability of TM helix-helix interactions has been studied for the prototype TM helical dimer model system, glycophorin A TM (GpATM) (Hong and Bowie 2011; Hong et al.

J Chromatogr B Anal Tech Biomed Life Sci 877(26):2836–2846 Huysmans GH, Baldwin SA, Brockwell DJ, Radford SE (2010) The transition state for folding of an outer membrane protein. 6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322(5905):1211–1217 Jefferson RE, Blois TM, Bowie JU (2013) Membrane proteins can have high kinetic stability. J Am Chem Soc 135(40):15183–15190 Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU (2009) Similar energetic contributions of packing in the core of membrane and water-soluble proteins.

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