Conformational studies on polypeptide models of collagen. Poly(Gly-Pro-Val), poly(Gly-Pro-Met), poly(Gly-Val-Pro) and poly(Gly-Met-Pro)
- 12 January 2009
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 29 (2) , 216-230
- https://doi.org/10.1111/j.1399-3011.1987.tb02248.x
Abstract
The title polytripeptides were synthesized and studied experimentally by circular dichroism, and theoretically, by quantum mechanical methods. With the exception of poly(Gly-Pro-Val), which was found to be essentially structureless in solution, the other polymers adopt folded conformations, most probably of type II .beta.-bends. Conclusions from theoretical studies were generally in agreement with the experiment results. In particular, it is noteworthy that the optimized (.vphi., .psi.) maps for poly(Gly-Pro-Met) showed the absolute minimum (.vphi. = 60.degree., .psi. = 0.degree.) located inside the .beta.II bend space.Keywords
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