Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum.
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 (C(4)), -octanoyl (C(8)), -decanoyl (C(10)), -dodecanoyl (C(12)) and -tetradecanoyl (C(14))-ACPs display marked changes in backbone HN, C(alpha) and C(beta) 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.
Upadhyay
Santosh Kumar
SK
National Institute of Immunology, Aruna Asaf Ali Marg, JNU Campus, New Delhi 110067, India.
Misra
Ashish
A
Surolia
Namita
N
Surolia
Avadhesha
A
Sundd
Monica
M
D000213:Acyl Carrier Protein / Q000737:chemistry*; D004926:Escherichia coli; D005227:Fatty Acids / Q000096:biosynthesis; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010963:Plasmodium falciparum / Q000737:chemistry*; D015800:Protozoan Proteins / Q000737:chemistry*
D000213:Acyl Carrier Protein; D005227:Fatty Acids; D015800:Protozoan Proteins