Turn conformations in peptides containing the -Xaa-Ser- sequence

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DOIResolve DOI: http://doi.org/10.1111/j.1399-3011.1996.tb01108.x
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TypeArticle
Journal titleInternational Journal of Peptide and Protein Research
Volume48
Issue1
Pages7178; # of pages: 8
AbstractThe conformations of the protected dipeptides Boc-L-Pro-L-Ser-NHMe, Boc-L-Pro-D-Ser-NHMe, BOC-L- val-~-Ser-NHMe and Boc-L-Val-D-Ser-NHMe have been explored through interpretation of their infrared spectra in CH,C12, DMSO and D,O solution. In CH’Cl, solution the formation of a ten-membered ring (8-turn) for each compound is signaled by characteristic shifts in both the urethane C=O and the terminal NH stretching frequencies. For each peptide, differences in the amide I absorption patterns for LL and LD isomers are consistent with the formation of type I and type zyxwvutsrqponmlkjihgfedcbaZYXWVUTSRQPONMLKJIHGFEDCBAI1 p-turns respectively in CH2C12 solution. The amide I absorptions suggest substantial disruption of intramolecular hydrogen bonding in DMSO, and no intermolecular hydrogen bonding whatsoever in aqueous solution. In CH2C12 solution the OH stretching vibration is consistent with the formation of a hydrogen bond to the C=O of the serine group; however, two additional absorptions at frequencies characteristic of ‘free’ OH groups also appear in all spectra. Implications regarding the serine in stabilizing the a-turn are discussed.>
Publication date
LanguageEnglish
AffiliationNRC Institute for Biodiagnostics; National Research Council Canada
Peer reviewedYes
NRC number418
NPARC number9148163
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Record identifierf9ff4b6f-1561-41d2-a0df-0791c2d9e6c8
Record created2009-06-25
Record modified2016-11-07
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