title: Protein stabilization by an amphiphilic short monodisperse oligo(ethylene glycol).
abstract: A short, monodisperse additive (octa(ethylene glycol) monophenyl ether) functions to suppress aggregation of thermally and chemically denatured lysozyme. Control studies with shorter and non-amphiphilic derivatives revealed that the amphiphilic structure is essential, and octa(ethylene glycol) is nearly the minimum chain length for amphiphilic poly(ethylene glycol)s to stabilize proteins.
authors: Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1, Katahira, Aoba-ku, Sendai 980-8577, Japan. kinbara@tagen.tohoku.ac.jp.
authors: Nabanita
authors: N
authors: Sadhukhan
authors: Takahiro
authors: T
authors: Muraoka
authors: Mihoko
authors: M
authors: Ui
authors: Satoru
authors: S
authors: Nagatoishi
authors: Kouhei
authors: K
authors: Tsumoto
authors: Kazushi
authors: K
authors: Kinbara
mesh_terms: D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D009113:Muramidase / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry*
chemical_list: D011092:Polyethylene Glycols; D009113:Muramidase