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RSS FeedsStructure of an Unfolding Intermediate of an RRM Domain of ETR-3 Reveals Its Native-like Fold (Biophysical Journal)

 
 

21 january 2020 22:00:19

 
Structure of an Unfolding Intermediate of an RRM Domain of ETR-3 Reveals Its Native-like Fold (Biophysical Journal)
 


Prevalence of one or more partially folded intermediates during protein unfolding with different secondary and ternary conformations has been identified as an integral character of protein unfolding. These transition-state species need to be characterized structurally for elucidation of their folding pathways. We have determined the three-dimensional structure of an intermediate state with increased conformational space sampling under urea-denaturing condition. The protein unfolds completely at 10 M urea but retains residual secondary structural propensities with restricted motion.


 
134 viewsCategory: Biophysics
 
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