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16875-10-8

16875-10-8 | Glycine, L-prolyl-L-prolyl-

CAS No: 16875-10-8 Catalog No: AG001Y9J MDL No:

Product Description

Catalog Number:
AG001Y9J
Chemical Name:
Glycine, L-prolyl-L-prolyl-
CAS Number:
16875-10-8
Molecular Formula:
C12H19N3O4
Molecular Weight:
269.2970
IUPAC Name:
2-[[(2S)-1-[(2S)-pyrrolidine-2-carbonyl]pyrrolidine-2-carbonyl]amino]acetic acid
InChI:
InChI=1S/C12H19N3O4/c16-10(17)7-14-11(18)9-4-2-6-15(9)12(19)8-3-1-5-13-8/h8-9,13H,1-7H2,(H,14,18)(H,16,17)/t8-,9-/m0/s1
InChI Key:
LEIKGVHQTKHOLM-IUCAKERBSA-N
SMILES:
OC(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1

Properties

Complexity:
385  
Compound Is Canonicalized:
Yes
Covalently-Bonded Unit Count:
1  
Defined Atom Stereocenter Count:
2  
Defined Bond Stereocenter Count:
0
Exact Mass:
269.138g/mol
Formal Charge:
0
Heavy Atom Count:
19  
Hydrogen Bond Acceptor Count:
5  
Hydrogen Bond Donor Count:
3  
Isotope Atom Count:
0
Molecular Weight:
269.301g/mol
Monoisotopic Mass:
269.138g/mol
Rotatable Bond Count:
4  
Topological Polar Surface Area:
98.7A^2
Undefined Atom Stereocenter Count:
0
Undefined Bond Stereocenter Count:
0
XLogP3:
-3  

Literature

Title Journal
Temperature-dependent higher order structures of the (Pro-Pro-Gly)₁₀-modified dendrimer. Biopolymers 20110401
Semax and Pro-Gly-Pro activate the transcription of neurotrophins and their receptor genes after cerebral ischemia. Cellular and molecular neurobiology 20100101
The effect of deuterium oxide on the stability of the collagen model peptides H-(Pro-Pro-Gly)(10)-OH, H-(Gly-Pro-4(R)Hyp)(9)-OH, and Type I collagen. Biopolymers 20100101
Catalytic removal of N-allyloxycarbonyl groups using the [CpRu(IV)(pi-C3H5)(2-quinolinecarboxylato)]PF6 complex. A new efficient deprotecting method in peptide synthesis. The Journal of organic chemistry 20060609
Conformation of alloHyp in the Y position in the host-guest peptide with the pro-pro-gly sequence: implication of the destabilization of (Pro-alloHyp-Gly)10. Biopolymers 20060215
Completely geometrically optimized DFT/ONIOM triple-helical collagen-like structures containing the ProProGly, ProProAla, ProProDAla, and ProProDSer triads. Journal of the American Chemical Society 20051019
Collagen-like triple helix formation of synthetic (Pro-Pro-Gly)10 analogues: (4(S)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10, (4(R)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10 and (4(S)-fluoroprolyl-4(R)-fluoroprolyl-Gly)10. Journal of peptide science : an official publication of the European Peptide Society 20051001
Repetitive interactions observed in the crystal structure of a collagen-model peptide, [(Pro-Pro-Gly)9]3. Journal of biochemistry 20050801
Unexpected puckering of hydroxyproline in the guest triplets, hyp-pro-gly and pro-allohyp-gly sandwiched between pro-pro-gly sequence. Chembiochem : a European journal of chemical biology 20050701
Studies of the collagen-like peptide (Pro-Pro-Gly)(10) confirm that the shape and position of the type I collagen denaturation endotherm is governed by the rate of helix unfolding. Journal of molecular biology 20040402
Asymmetry in the triple helix of collagen-like heterotrimers confirms that external bonds stabilize collagen structure. Journal of molecular biology 20030523
Understanding the role of stereoelectronic effects in determining collagen stability. 2. A quantum mechanical/molecular mechanical study of (Proline-Proline-Glycine)(n) polypeptides. Journal of the American Chemical Society 20020703
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)(10)](3). Protein science : a publication of the Protein Society 20020201
Adhesion of N-methacryloyl-omega-amino acid primers to collagen analyzed by 13C NMR. Journal of dental research 20010301

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