Conformational and ion binding properties of a cyclic octapeptide, cyclo (Ala-Leu-Pro-Gly)2.
The conformation and ion-binding characteristics of a cyclic octapeptide, cyclo (Ala-Leu-Pro-Gly)2, in a liphophilic solvent, acetonitrile, have been studied using CD and nmr spectroscopy. The peptide binds preferentially to divalent cations such as calcium, magnesium, and barium. The conformations of the free cyclic peptide and its calcium complex are very similar with well-defined beta- and gamma-turns. The cyclic peptide readily forms equimolar and possibly 2:1 (peptide:cation) complexes with divalent cations.
Jois
D S
DS
Molecular Biophysics Unit, Indian Institute of Science, Bangalore.
Easwaran
K R
KR
Bednarek
M
M
Blout
E R
ER
D000595:Amino Acid Sequence; D002942:Circular Dichroism; D007477:Ions; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
D007477:Ions; D010456:Peptides, Cyclic; C077930:cyclo(alanyl-leucyl-prolyl-glycyl)2