Conformation of model, alanine and proline containing tetrapeptides in water
- 1 March 1983
- journal article
- research article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 21 (3) , 301-306
- https://doi.org/10.1111/j.1399-3011.1983.tb03108.x
Abstract
CD [circular dichroism] spectra of model alanine and prolyl-alanine tetrapeptides were measured at different pH values. An analysis of the spectra shows that proline in position 2 or 4 of a tetrapeptide favors folding of the peptide chain, and unfolding when it is in position 3. Changes in CD spectra evidence growing amounts of the .beta.-turn conformation upon increasing pH, independent of proline position in the peptide chain.Keywords
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