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

R. A. Shaw, A. Perczel, G. D. Fasman, H. H. Mantsch

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The conformations of the protected dipeptides Boc-L-Pro-L-Ser-NHMe, Boc-L-Pro-D-Ser-NHMe, BOC-L-Val-L-Ser-NHMe and Boc-L-Val-D-Ser-NHMe have been explored through interpretation of their infrared spectra in CH2Cl2, DMSO and D2O solution. In CH2Cl2 solution the formation of a ten-membered ring (β-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 II β-turns respectively in CH2Cl2 solution. The amide I absorptions suggest substantial disruption of intramolecular hydrogen bonding in DMSO, and no intermolecular hydrogen bonding whatsoever in aqueous solution. In CH2Cl2 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 β-turn are discussed.

Original languageEnglish
Pages (from-to)71-78
Number of pages8
JournalInternational Journal of Peptide and Protein Research
Volume48
Issue number1
Publication statusPublished - 1996

Fingerprint

Conformations
Peptides
Hydrogen bonds
Hydrogen Bonding
Dimethyl Sulfoxide
Amides
Serine
Stretching
Dipeptides
Urethane
Vibration
Isomers
Hydrogen
Infrared radiation
serine containing aminolipid

Keywords

  • Conformation
  • Infrared spectroscopy
  • Serine
  • Turns

ASJC Scopus subject areas

  • Biochemistry

Cite this

Turn conformations in peptides containing the -Xaa-Ser- sequence. / Shaw, R. A.; Perczel, A.; Fasman, G. D.; Mantsch, H. H.

In: International Journal of Peptide and Protein Research, Vol. 48, No. 1, 1996, p. 71-78.

Research output: Contribution to journalArticle

Shaw, R. A. ; Perczel, A. ; Fasman, G. D. ; Mantsch, H. H. / Turn conformations in peptides containing the -Xaa-Ser- sequence. In: International Journal of Peptide and Protein Research. 1996 ; Vol. 48, No. 1. pp. 71-78.
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AB - The conformations of the protected dipeptides Boc-L-Pro-L-Ser-NHMe, Boc-L-Pro-D-Ser-NHMe, BOC-L-Val-L-Ser-NHMe and Boc-L-Val-D-Ser-NHMe have been explored through interpretation of their infrared spectra in CH2Cl2, DMSO and D2O solution. In CH2Cl2 solution the formation of a ten-membered ring (β-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 II β-turns respectively in CH2Cl2 solution. The amide I absorptions suggest substantial disruption of intramolecular hydrogen bonding in DMSO, and no intermolecular hydrogen bonding whatsoever in aqueous solution. In CH2Cl2 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 β-turn are discussed.

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