Circular dichroism conformational study of the chemotactic peptide formyl‐L‐methionyl‐L‐leucyl‐L‐phenylalanine
- 1 February 1982
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 19 (2) , 133-136
- https://doi.org/10.1111/j.1399-3011.1982.tb02600.x
Abstract
The solution circular dichroism [CD] of the chemotactic agent formyl-L-methionyl-L-leucyl-L-phenylalanine was highly solvent-dependent. In relatively nonpolar solvents (fluoroalcohols) the CD is that characteristic of a folded conformation. In H2SO4 the tripeptide remains intact and displays a CD typical of highly solvated and totally disordered peptides. The order-to-disorder transition can be followed by addition of water to trifluoroethanol.Keywords
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