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RSS FeedsA dynamic hydrophobic core and surface salt bridges thermostabilize a designed three-helix bundle (Biophysical Journal)

 
 

16 january 2019 01:00:05

 
A dynamic hydrophobic core and surface salt bridges thermostabilize a designed three-helix bundle (Biophysical Journal)
 


Thermostable proteins are advantageous in industrial applications, as pharmaceuticals or biosensors, and as templates for directed evolution. As protein design methodologies improve, bioengineers are able to design proteins to perform a desired function. While many rationally designed proteins end up being thermostable, how to intentionally design de novo, thermostable proteins is less clear. UVF is a de novo designed protein based on the backbone structure of the Engrailed homeodomain (EnHD) and is highly thermostable (Tm > 99°C vs.


 
77 viewsCategory: Biophysics
 
Non-sinusoidal waveform in temperature-compensated circadian oscillations (Biophysical Journal)
Fold-change detection of NF-?B at target genes with different transcript outputs (Biophysical Journal)
 
 
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