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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Extra resources for Lipids in Protein Misfolding
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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.
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