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About This Item
经验公式（希尔记法）:
C21H30N6O6
CAS号:
分子量:
462.50
MDL编号:
UNSPSC代码:
12352202
PubChem化学物质编号:
NACRES:
NA.26
product name
Cyclo(Pro-Gly)3, ≥97% (HPLC)
检测方案
≥97% (HPLC)
形式
solid
储存温度
−20°C
SMILES字符串
O=C1CNC(=O)C2CCCN2C(=O)CNC(=O)C3CCCN3C(=O)CNC(=O)C4CCCN14
InChI
1S/C21H30N6O6/c28-16-10-23-20(32)14-5-2-9-27(14)18(30)12-24-21(33)15-6-3-8-26(15)17(29)11-22-19(31)13-4-1-7-25(13)16/h13-15H,1-12H2,(H,22,31)(H,23,32)(H,24,33)
InChI key
WAOABPNIJIPSKM-UHFFFAOYSA-N
生化/生理作用
Model peptide that binds Ca2+ with an affinity comparable to that of naturally-occurring Ca2+-binding proteins
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
L M Thomas et al.
Biopolymers, 34(8), 1007-1013 (1994-08-01)
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
G Kartha et al.
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
K I Varughese et al.
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
I M Asher et al.
Biochemistry, 19(9), 1805-1813 (1980-04-29)
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
F Sussman et al.
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
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