Circular dichroism study of poly(l-tyrosine), poly(l-glutamic acid) and of random and sequential copolymers of l-glutamic acid and l-tyrosine in trimethylphosphate |
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Authors: | Yves Trudelle Gérard Spach |
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Affiliation: | Centre de Biophysique Moléculaire, CNRS, 45045 Orléans-Cedex, France |
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Abstract: | Random and sequential copolypeptides containing l-glutamic acid and l-tyrosine, as well as poly(l-tyrosine) and poly(l-glutamic acid) were investigated by means of c.d. spectroscopy in trimethylphosphate as solvent. In random copolymers, variation of ellipticities at 202.5 and 230 nm versus tyrosyl content follows a smooth curve, without any sharp change. This led to the conclusion that poly(l-tyrosine) α-helix is right-handed. From c.d. studies on sequential copolymers we were able to recognize that the 230 nm contribution of tyrosyl side chains is closely related to the array in which tyrosyl residues are arranged in the chain. For instance, it was found that (n, n + 2) and (n, n + 3) pairings of tyrosyl side-chains in (Tyr-Glu)n and (Glu-Tyr-Glu)n respectively, were poorly effective, while the (n, n + 4) pairing in (Glu-Glu-Tyr-Glu)n is more. However, the strongest contribution at 230 nm was observed on the alternating-páirs copolymer (Glu-Tyr-Tyr-Glu)n. This result suggests a new conformational arrangement of tyrosyl side chains in sequential copolymers, as well as in poly(l-tyrosine) and other aromatic polypeptides, based on a regular pairing of the aromatic groups, arranged in two contiguous superhelices. |
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