Conformation of model, alanine and proline containing tetrapeptides in water. Comparison of 13C-n.m.r. and CD results.
作者信息
Lisowski M, Siemion I Z, Sobczyk K
出版信息
Int J Pept Protein Res. 1983 Mar;21(3):301-6. doi: 10.1111/j.1399-3011.1983.tb03108.x.
Abstract
CD 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 favours 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.
摘要
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