Journal
BIOPOLYMERS
Volume 69, Issue 2, Pages 270-281Publisher
JOHN WILEY & SONS INC
DOI: 10.1002/bip.10354
Keywords
polyproline II; left-handed helix; 3(1)-helix; CD; NMR; chemical shifts; scalar coupling constants
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Funding
- NIA NIH HHS [R3AG14179A] Funding Source: Medline
- PHS HHS [206191] Funding Source: Medline
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NMR characteristics of a model left-handed 3(1)-helical peptide are reported in this study. With temperature and sequence corrections on the predicted random coil N-15 chemical shifts, a significant N-15 chemical shift deviation is observed for the model 3, peptide. The N-15 chemical shift differences also correlate well with the molar ellipticities (at 220 nm) of the CD spectra at different temperatures, indicating that the N-15 chemical shift is a sensitive probe for 3(1)-helices. The average (3)J(HNalpha) and 1J(CalphaHalpha) values of the model peptide are determined to be 65 and 142.6 Hz, respectively, which are consistent with the values calculated from the geometry of 3(1)-helices. With careful measurements of amide N-15 chemical shifts and incorporating temperature and sequence effect corrections, the N-15 chemical shifts can be used together with (3)J(HNalpha) and (1)J(CalphaHalpha) to differentiate 3(1)-helices from random coils with high confidence. Based on the observed NMR characteristics, a strategy is developed for probing left-handed 3(1)-helical structures from other secondary structures. (C) 2003 Wiley Periodicals, Inc.
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