The crystal structure of cyclo(Pro-Gly)3 (PG3) complex with LiSCN (C22H30N7O6SLi) has been solved by x-ray diffraction. The crystals belong to the space group R3 in the hexagonal setting with unit cell parameters of a = 12.581(1), c = 29.705(3) A
Raman spectra of the cyclic hexapeptide cyclo-(L-prolylglycyl)3 and its Na+, K+, and Ca2+ complexes are reported for the solid state and for samples in solution. Model compounds and N-deuteration were used to aid mode identification. Spectra of the uncomplexed ionophore
International journal of peptide and protein research, 27(2), 112-117 (1986-02-01)
The crystal structure of cyclo(L-Pro-Gly)3 was solved using X-ray crystallographic techniques. The backbone of the peptide is asymmetric and is made up of five trans peptide units and one cis peptide. There is a hydrogen bonded water bridge that links
Proceedings of the National Academy of Sciences of the United States of America, 86(20), 7880-7884 (1989-10-01)
Calcium plays a crucial role in many cellular processes. Its functions are directly dependent on the high specificity for Ca2+ exhibited by the proteins and ion carriers that bind divalent ions. To elucidate the basis for this specificity we have
International journal of peptide and protein research, 27(2), 118-122 (1986-02-01)
The synthetic cyclic hexapeptide (L-prolyl-glycyl)3 forms a 2:1 complex with Ca2+ ion. The cation is sandwiched between the two peptide molecules. The glycyl carbonyls from each of the peptides are octahedrally coordinated to the cation with an average calcium oxygen
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