ArticleEuropean biophysics journal : EBJ2016
The role of an L-leucine residue on the conformations of glycyl-L-leucine oligomers and its N- or C-terminal dependence: infrared absorption and Raman scattering studies.
Article in European biophysics journal : EBJ, 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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1 citing paper in PubMed.
- Fourier-transform infrared spectroscopy for monitoring proteolytic reactions using dry-films treated with trifluoroacetic acid.Scientific reports · 2020Article
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Abstract
The conformations of glycyl-L-leucine oligomers (GnL, residue number n = 3, 4, and 5) in the solid state were found to be similar to that of a polyglycine II (PGII). However, for L-leucyl-glycine oligomers (LGn; n = 3, 4, 5) in the solid state, LG3 and LG4 have already been confirmed to take a reverse-turn structure (LG3-type reverse-turn) while LG5 adopts a PGII-type helix. The present results provide evidence that the conformations of L-leucine-containing glycine oligomers depend strongly upon whether the L-leucine residue is placed in the N- or C-terminal position. For the aqueous G3L and G4L samples, we assumed that reverse-turn structures similar to the type II β-turn, rather than the LG3-type reverse-turn, are stabilized in concentrated solution, probably as the result of aggregation. Models to explain the mechanism of these phenomena are presented.
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