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

Target

Families : PEG-4000 ligand of proteins in family
6_AlphaBeta_hydrolase

Structure :
4HS9 3VIS 2ZYR

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 :
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 :
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 :
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 :
PubMedSearch : Chen_2009_J.Mol.Biol_390_672
PubMedID: 19447113
Gene_locus related to this paper: arcfu-AF1763