Article

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

  • Santosh Kumar UpadhyayAffiliated withNational Institute of Immunology
  • , Ashish MisraAffiliated withMolecular Biophysics Unit, Indian Institute of Science
  • , Namita SuroliaAffiliated withMolecular Biology and Genetics Unit, Jawaharlal Nehru Center for Advanced Scientific Research
  • , Avadhesha SuroliaAffiliated withNational Institute of ImmunologyMolecular Biophysics Unit, Indian Institute of Science
  • , Monica SunddAffiliated withNational Institute of Immunology Email author 

Rent the article at a discount

Rent now

* Final gross prices may vary according to local VAT.

Get Access

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 assignments Acyl-ACPs Plasmodium falciparum Fatty acid biosynthesis