ArticleProtein science : a publication of the Protein Society2016
Folding recombinant spider-silk in H2 O: Effect of osmolytes on the solution conformation of a 15-repeat spider-silk mimetic.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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3 authors at 1 institution in 1 country.
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Abstract
The folding of a recombinant spider silk protein-polymer in the presence of the tri-methylamine osmolytes TMANO and Betaine in 80% H2 O is reported. Circular dichroism measurements (CD) reveal an increase in α-helical secondary structure with increasing osmolyte concentrations, as determined by an increase in ellipticity at 222 nm. Consistent with this observation, the signal for random coil sampling, observed at 205 nm, is greatly reduced with increasing trimethylamine. Fluorescence spectra of a single tyrosine positioned within the conserved 33-amino acid repeat primary sequence (of the spider-silk mimetic) complements the conformational changes observed by CD. Importantly, there is a correlation between the number of Alkyl-groups (CH3 -) on the amine of the osmolyte and enhanced helicity of the 15-repeat silk-mimetic for the osmolytes tested, ie TMANO, Betaine, Sarcosine and Glycine. These preliminary results are applicable to storing and processing recombinant silk sequences in H2 O, an important mile-stone for widespread use of recombinant silk polymers.
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