1H NMR study on the conformation of bacitracin A in aqueous solution.
The conformation of bacitracin A, a widely used cyclic dodecapeptide antibiotic in aqueous solution, has been investigated using 500 MHz 1H NMR and molecular modeling. Findings revealed that a region (residues 1-6) is folded over the cyclic ring, resulting in metal coordination sites, a thiazoline ring, and Glu4 and His10 being proximate to each other.
Kobayashi
N
N
Institute of Applied Biochemistry, University of Tsukuba, Japan.
Takenouchi
T
T
Endo
S
S
Munekata
E
E
D000595:Amino Acid Sequence; D001414:Bacitracin / Q000031:analogs & derivatives* / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation
D001414:Bacitracin; C026461:bacitracin A