Journal of Biomolecular NMR

, Volume 5, Issue 1, pp 67–81

1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

  • David S. Wishart
  • Colin G. Bigam
  • Arne Holm
  • Robert S. Hodges
  • Brian D. Sykes
Research Paper

DOI: 10.1007/BF00227471

Cite this article as:
Wishart, D.S., Bigam, C.G., Holm, A. et al. J Biomol NMR (1995) 5: 67. doi:10.1007/BF00227471

Summary

In this study we report on the 1H, 13C and 15N NMR chemical shifts for the random coil state and nearest-neighbor sequence effects measured from the protected linear hexapeptide Gly-Gly-X-Y-Gly-Gly (where X and Y are any of the 20 common amino acids). We present data for a set of 40 peptides (of the possible 400) including Gly-Gly-X-Ala-Gly-Gly and Gly-Gly-X-Pro-Gly-Gly, measured under identical aqueous conditions. Because all spectra were collected under identical experimental conditions, the data from the Gly-Gly-X-Ala-Gly-Gly series provide a complete and internally consistent set of 1H, 13C and 15N random coil chemical shifts for all 20 common amino acids. In addition, studies were also conducted into nearest-neighbor effects on the random coil shift arising from a variety of X and Y positional substitutions. Comparisons between the chemical shift measurements obtained from Gly-Gly-X-Ala-Gly-Gly and Gly-Gly-X-Pro-Gly-Gly reveal significant systematic shift differences arising from the presence of proline in the peptide sequence. Similarly, measurements of the chemical shift changes occurring for both alanine and proline (i.e., the residues in the Y position) are found to depend strougly on the type of amino acid substituted into the X position. These data lend support to the hypothesis that sequence effects play a significant role in determining peptide and protein chemical shifts.

Keywords

1H, 13C, 15N NMR chemical shiftsRandom coilAmino acidPeptide

Abbreviations

DIEA

diisopropylethylamine

DMF

dimethylformamide

DMSO

dimethyl sulfoxide

DSS

2,2-dimethyl-2-silapentane-5-sulfonic acid

HMQC

heteronuclear multiple-quantum coherence

HOBt

N-hydroxybenzotriazole

MBHA

4-methylbenzyhydrylamine

NOE

nuclear Overhauser effect

TBTU

2-(benzotriazole-1-yl)-1,1,3,3-tetramethyluronium tetrafluoroborate

TFE

trifluoroethanol

TMS

tetramethylsilane

TOCSY

total correlation spectroscopy

TSP

3-(trimethylsilyl)propionate, sodium salt

Copyright information

© ESCOM Science Publishers B.V. 1995

Authors and Affiliations

  • David S. Wishart
    • 1
  • Colin G. Bigam
    • 1
  • Arne Holm
    • 1
  • Robert S. Hodges
    • 1
  • Brian D. Sykes
    • 1
  1. 1.Protein Engineering Network of Centres of Excellence, Department of BiochemistryUniversity of AlbertaEdmontonCanada
  2. 2.Chemistry DepartmentRoyal Veterinary and Agriculture UniversityFrederiksbergDenmark