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- W2031196713 abstract "Hutchinson-Gilford progeria syndrome (HGPS) is a premature aging disease caused by the expression and accumulation of a mutant lamin A protein, progerin. We report experimental and computational results that characterize the biophysical stability of lamin A and progerin tail domains which are mostly disordered. We study protein unfolding with increasing temperature using tryptophan fluorescence and circular dichroism of purified, recombinant wild type (wt) and progerin tail domains. Both methods indicate that the progerin tail has a higher transition melting temperature than its wt counterpart. Replica Exchange Molecular Dynamics (REMD) simulations predict the progerin tail to be a more compact structure. Simulated forced protein unfolding confirm our experimental results; where the predicted energy to unfold the progerin tail is higher than the wt lamin A tail. Also, the structural simulations of wt lamin tail show that the main site for proteolysis during normal posttranslational modification of lamin A is an unfolded region located on a loop on the periphery of all the predicted protein configurations, suggesting its ample accessibility to proteolysis. Progerin lacks this region for posttranslational proteolysis, but its further compactness suggests a more general resistance to turnover and more stable filament structures, as previously observed, potentially leading to the toxic accumulation observed in disease. We also believe that this combination of experimental results and REMD simulations is a useful method of studying structure of disordered proteins." @default.
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- W2031196713 date "2011-02-01" @default.
- W2031196713 modified "2023-09-28" @default.
- W2031196713 title "Insights Into the Structure and Mechanics of a Mostly Disordered Protein: Lamin A and Progerin Tail Domians" @default.
- W2031196713 doi "https://doi.org/10.1016/j.bpj.2010.12.1226" @default.
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