Biomolecular NMR Assignments

, Volume 4, Issue 1, pp 83–85

Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum

Authors

  • Santosh Kumar Upadhyay
    • National Institute of Immunology
  • Ashish Misra
    • Molecular Biophysics UnitIndian Institute of Science
  • Namita Surolia
    • Molecular Biology and Genetics UnitJawaharlal Nehru Center for Advanced Scientific Research
  • Avadhesha Surolia
    • National Institute of Immunology
    • Molecular Biophysics UnitIndian Institute of Science
    • National Institute of Immunology
Article

DOI: 10.1007/s12104-010-9212-2

Cite this article as:
Upadhyay, S.K., Misra, A., Surolia, N. et al. Biomol NMR Assign (2010) 4: 83. doi:10.1007/s12104-010-9212-2

Abstract

We report the backbone chemical shift assignments of the acyl-acyl carrier protein (ACP) intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum. The acyl-ACP intermediates butyryl (C4), -octanoyl (C8), -decanoyl (C10), -dodecanoyl (C12) and -tetradecanoyl (C14)-ACPs display marked changes in backbone HN, Cα and Cβ chemical shifts as a result of acyl chain insertion into the hydrophobic core. Chemical shift changes cast light on the mechanism of expansion of the acyl carrier protein core.

Keywords

Backbone assignmentsAcyl-ACPsPlasmodium falciparumFatty acid biosynthesis

Copyright information

© Springer Science+Business Media B.V. 2010