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10.1016/j.bpj.2014.09.008 http://scihub22266oqcxt.onion/10.1016/j.bpj.2014.09.008 C4213668!4213668!25418175     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Biophys+J 2014 ; 107 (8): 1939-49 Nephropedia Template TP {{tp|p=25418175|t=2014. Amyloid Fibrillation of Insulin under Water-Limited Conditions |pdf=|usr=}}{{25418175}} gab.com Text Amyloid Fibrillation of Insulin under Water-Limited Conditions JO: Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25418175 #FOAvip Amyloid fibrillation in water-organic mixtures has been widely studied to understand the effect of protein-solvent interactions on the fibrillation process. In this study, we monitored insulin fibrillation in formamide and its methyl derivatives (formamide, N-methyl formamide, N,N-dimethyl formamide) in the presence and absence of water. These model solvent systems mimic the cellular environment by providing denaturing conditions and a hydrophobic environment with limited water content. Thioflavin T (ThT) assay revealed that binary mixtures of water with formamide and its methyl derivatives enhanced fibrillation rates and ?-sheet abundance, whereas organic solvents suppressed insulin fibrillation. We utilized solution small-angle x-ray scattering (SAXS) and differential scanning calorimetry (DSC) to investigate the correlation between protein-solvent interactions and insulin fibrillation. SAXS experiments combined with simulated annealing of the protein indicated that the degree of denaturation of the hydrophobic core region at residues B11?B17 determines the fibrillation rate. In addition, DSC experiments suggested a crucial role of hydrophobic interactions in the fibrillation process. These results imply that an environment with limited water, which imitates a lipid membrane system, accelerates protein denaturation and the formation of intermolecular hydrophobic interactions during amyloid fibrillation. Twit Text FOAVip Amyloid Fibrillation of Insulin under Water-Limited Conditions ????Biophys J http://www.kidney.de/pget.php?&tw=1&pmid=25418175 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25418175 #FOAvip English Wikipedia <ref>{{Cite pmid|25418175}}</ref> Amyloid Fibrillation of Insulin under Water-Limited Conditions #MMPMID25418175 Choi T; Lee J; Jin K; Kim H Biophys J 2014[Oct]; 107 (8): 1939-49 PMID25418175show ga Amyloid fibrillation in water-organic mixtures has been widely studied to understand the effect of protein-solvent interactions on the fibrillation process. In this study, we monitored insulin fibrillation in formamide and its methyl derivatives (formamide, N-methyl formamide, N,N-dimethyl formamide) in the presence and absence of water. These model solvent systems mimic the cellular environment by providing denaturing conditions and a hydrophobic environment with limited water content. Thioflavin T (ThT) assay revealed that binary mixtures of water with formamide and its methyl derivatives enhanced fibrillation rates and ?-sheet abundance, whereas organic solvents suppressed insulin fibrillation. We utilized solution small-angle x-ray scattering (SAXS) and differential scanning calorimetry (DSC) to investigate the correlation between protein-solvent interactions and insulin fibrillation. SAXS experiments combined with simulated annealing of the protein indicated that the degree of denaturation of the hydrophobic core region at residues B11?B17 determines the fibrillation rate. In addition, DSC experiments suggested a crucial role of hydrophobic interactions in the fibrillation process. These results imply that an environment with limited water, which imitates a lipid membrane system, accelerates protein denaturation and the formation of intermolecular hydrophobic interactions during amyloid fibrillation. äAmyloid Fibrillation of Insulin under Water-Limited Conditions (epmc).pdf DeepDyve Pubget Overpricing