65 research outputs found
Protein repellent hydrophilic grafts prepared by surface-initiated atom transfer radical polymerization from polypropylene
Crystal structure of a soluble form of the intracellular chloride ion channel CLIC1 (NCC27) at 1.4-A resolution.
Abstract CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exists in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to those observed in vivo. The structure of the soluble form of CLIC1 has been determined at 1.4-A resolution. The protein is monomeric and structurally homologous to the glutathioneS-transferase superfamily, and it has a redox-active site resembling glutaredoxin. The structure of the complex of CLIC1 with glutathione shows that glutathione occupies the redox-active site, which is adjacent to an open, elongated slot lined by basic residues. Integration of CLIC1 into the membrane is likely to require a major structural rearrangement, probably of the N-domain (residues 1–90), with the putative transmembrane helix arising from residues in the vicinity of the redox-active site. The structure indicates that CLIC1 is likely to be controlled by redox-dependent processes
Thermoresponsive Reversible Behavior of Multistimuli Pluronic-Based Pentablock Copolymer at the Air−Water Interface
Modulating the biocompatibility of polymer surfaces with poly(ethylene glycol): Effect of fibronectin
Control of protein/cell interactions with polymer surfaces via photo-grafting of poly(ethylene glycol) (PEG)
Modulating the biocompatibility of polymer surfaces with poly(ethylene glycol) – Effect of fibronectin
Low bacterial attachment to coatings produced by low energy plasma polymerization
Abstract not available
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