PEG-4000
Polyethylene glycol (PEG) is a polyether compound with many applications from industrial manufacturing to medicine. PEG is also known as polyethylene oxide (PEO) or polyoxyethylene (POE), depending on its molecular weight. The structure of PEG is commonly expressed as H-(O-CH2-CH2)n-OH. The numbers that are often included in the names of PEGs indicate their average molecular weights (e.g. a PEG with n = 9 would have an average molecular weight of approximately 400 daltons, and would be labeled PEG 400.) PEG-200 n =4 190 - 210 g/mol
General
Type : Polymer,Poly-ethylene-glycol
Chemical_Nomenclature : 2-[2-[2-[2-[2-[2-(2-ethoxyethoxy)ethoxy]ethoxy]ethoxy]ethoxy]ethoxy]ethanol
Canonical SMILES : CCOCCOCCOCCOCCOCCOCCOCCO
InChI : InChI=1S\/C16H34O8\/c1-2-18-5-6-20-9-10-22-13-14-24-16-15-23-12-11-21-8-7-19-4-3-17\/h17H,2-16H2,1H3
InChIKey : PJWQOENWHPEPKI-UHFFFAOYSA-N
Other name(s) : PEG4000,PEG4K,PE4,Heptaethylene glycol monoethyl ether,3,6,9,12,15,18,21-Heptaoxatricosan-1-ol,2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol,4435-25-0,Polyethylene glycol PEG4000
MW : 354.44
Formula : C16H34O8
CAS_number :
PubChem : 448032
UniChem : PJWQOENWHPEPKI-UHFFFAOYSA-N
IUPHAR :
Wikipedia :
Target
Families : PEG-4000 ligand of proteins in family: 6_AlphaBeta_hydrolase
Stucture :
Protein : arcfu-AF1763
References (4)
| Title : Dieselzymes: development of a stable and methanol tolerant lipase for biodiesel production by directed evolution. - Korman_2013_Biotechnol.Biofuels_6_70 |
| Author(s) : Korman TP , Sahachartsiri B , Charbonneau DM , Huang GL , Beauregard M , Bowie JU |
| Ref : Biotechnol Biofuels , 6 :70 , 2013 |
| Abstract : Korman_2013_Biotechnol.Biofuels_6_70 |
| ESTHER : Korman_2013_Biotechnol.Biofuels_6_70 |
| PubMedSearch : Korman_2013_Biotechnol.Biofuels_6_70 |
| PubMedID: 23648063 |
| Gene_locus related to this paper: promi-c2lfd0 |
| Title : Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76A resolution - Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
| Author(s) : Kitadokoro K , Thumarat U , Nakamura R , Nishimura K , Karatani H , Suzuki H , Kawai F |
| Ref : Polymer Degradation and Stability , 97 :771 , 2012 |
| Abstract : Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
| ESTHER : Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
| PubMedSearch : Kitadokoro_2012_Polym.Degrad.Stab_97_771 |
| PubMedID: |
| Gene_locus related to this paper: 9acto-f7ix06 |
| Title : Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119 - Thumarat_2012_Appl.Microbiol.Biotechnol_95_419 |
| Author(s) : Thumarat U , Nakamura R , Kawabata T , Suzuki H , Kawai F |
| Ref : Applied Microbiology & Biotechnology , 95 :419 , 2012 |
| Abstract : Thumarat_2012_Appl.Microbiol.Biotechnol_95_419 |
| ESTHER : Thumarat_2012_Appl.Microbiol.Biotechnol_95_419 |
| PubMedSearch : Thumarat_2012_Appl.Microbiol.Biotechnol_95_419 |
| PubMedID: 22183084 |
| Gene_locus related to this paper: 9acto-f7ix06 |
| Title : Structure of the alkalohyperthermophilic Archaeoglobus fulgidus lipase contains a unique C-terminal domain essential for long-chain substrate binding - Chen_2009_J.Mol.Biol_390_672 |
| Author(s) : Chen CK , Lee GC , Ko TP , Guo RT , Huang LM , Liu HJ , Ho YF , Shaw JF , Wang AH |
| Ref : Journal of Molecular Biology , 390 :672 , 2009 |
| Abstract : Chen_2009_J.Mol.Biol_390_672 |
| ESTHER : Chen_2009_J.Mol.Biol_390_672 |
| PubMedSearch : Chen_2009_J.Mol.Biol_390_672 |
| PubMedID: 19447113 |
| Gene_locus related to this paper: arcfu-AF1763 |