@article {741,
	title = {Investigating the effect of increasing charge density on the hemolytic activity of synthetic antimicrobial polymers.},
	journal = {Biomacromolecules},
	volume = {9},
	year = {2008},
	month = {2008 Oct},
	pages = {2805-10},
	abstract = {The current study is aimed at investigating the effect of fine-tuning the cationic character of synthetic mimics of antimicrobial peptides (SMAMPs) on the hemolytic and antibacterial activities. A series of novel norbornene monomers that carry one, two, or three Boc-protected amine functionalities was prepared. Ring-opening metathesis polymerization (ROMP) of the monomers, followed by deprotection of the amine groups resulted in cationic antimicrobial polynorbornenes that carry one, two, and three charges per monomer repeat unit. Increasing the number of amine groups on the most hydrophobic polymer reduced its hemolytic activity significantly. To understand the membrane activity of these polymers, we conducted dye leakage experiments on lipid vesicles that mimic bacteria and red blood cell membranes, and these results showed a strong correlation with the hemolysis data.},
	keywords = {Amines, Anti-Infective Agents, Antimicrobial Cationic Peptides, Chemistry, Pharmaceutical, Drug Design, Erythrocytes, Escherichia coli, Hemolysis, Humans, Lipids, Magnetic Resonance Spectroscopy, Models, Chemical, Peptides, Polymers, Staphylococcus aureus},
	issn = {1526-4602},
	doi = {10.1021/bm800569x},
	author = {Al-Badri, Zoha M and Som, Abhigyan and Lyon, Sarah and Nelson, Christopher F and N{\"u}sslein, Klaus and Tew, Gregory N}
}
@article {541,
	title = {The structure of the core region of the lipopolysaccharide from Geobacter sulfurreducens.},
	journal = {Carbohydr Res},
	volume = {339},
	year = {2004},
	month = {2004 Dec 27},
	pages = {2901-4},
	abstract = {The structure of the core part of the LPS from Geobacter sulfurreducens was analysed. The LPS contained no O-specific polysaccharide (O-side chain) and upon mild hydrolysis gave a core oligosaccharide, which was isolated by gel chromatography. It was studied by chemical methods, NMR and mass spectrometry, and the following structure was proposed. [carbohydrate structure: see text] where Q = 3-O-Me-alpha-L-QuiNAc-(1-->or H (approximately 3:2).},
	keywords = {Carbohydrate Sequence, Geobacter, Lipopolysaccharides, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Oligosaccharides},
	issn = {0008-6215},
	doi = {10.1016/j.carres.2004.10.004},
	author = {Vinogradov, Evgeny and Korenevsky, Anton and Lovley, Derek R and Beveridge, Terry J}
}
@article {864,
	title = {In vitro polymerization and copolymerization of 3-hydroxypropionyl-CoA with the PHB synthase from Ralstonia eutropha.},
	journal = {Biomacromolecules},
	volume = {1},
	year = {2000},
	month = {2000 Fall},
	pages = {433-9},
	abstract = {The poly(3-hydroxybutyrate) (PHB) synthase of Ralstonia eutropha, which was produced by a recombinant strain of Escherichia coli and purified in one step with a methyl-HIC column to a purity of more than 90\%, was used to polymerize 3-hydroxypropionyl-CoA (3HPCoA) and to copolymerize 3HPCoA with 3-hydroxybutyryl-CoA (3HBCoA). A Km of 189 microM and a kcat of 10 s-1 were determined for the activity of the enzyme in the polymerization reaction of 3HPCoA based on the assumption that the dimer form of PHB synthase was the active form. Free coenzyme A was found to be a very effective competitive inhibitor for the polymerization of 3HPCoA with a Ki of 85 microM. The maximum degree of conversion of 3HPCoA to polymer was less than 40\%. In the simultaneous copolymerization reactions of these two monomers, both the turnover number for the copolymerization reaction and the maximum degree of conversion of 3HPCoA and 3HBCoA to copolymers increased with an increase in the amount of 3HBCoA in the monomer mixture. However, the maximum conversion of 3HPCoA to copolymer was always less than 35\%, regardless of the ratio of 3HPCoA to 3HBCoA. Block copolymers were obtained by the sequential copolymerization of the two monomers and these copolymers had a much narrower molecular weight distribution than those obtained by the simultaneous copolymerization for the same molar ratio of 3HPCoA to 3HBCoA.},
	keywords = {Acyltransferases, Coenzyme A, Escherichia coli, Kinetics, Magnetic Resonance Spectroscopy, Molecular Weight},
	issn = {1525-7797},
	author = {Song, J J and Zhang, S and Lenz, R W and Goodwin, S}
}
@article {1710,
	title = {Delineation of the intimate details of the backbone conformation of pyridine nucleotide coenzymes in aqueous solution.},
	journal = {Biochem Biophys Res Commun},
	volume = {66},
	year = {1975},
	month = {1975 Oct 27},
	pages = {1173-9},
	keywords = {Fourier Analysis, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Conformation, NAD, NADP, Structure-Activity Relationship, Temperature},
	issn = {0006-291X},
	author = {Bose, K S and Sarma, R H}
}
@article {1719,
	title = {Metal substitutions incarbonic anhydrase: a halide ion probe study.},
	journal = {Biochem Biophys Res Commun},
	volume = {66},
	year = {1975},
	month = {1975 Oct 27},
	pages = {1281-6},
	keywords = {Animals, Binding Sites, Cadmium, Carbonic Anhydrases, Cattle, Humans, Hydrogen-Ion Concentration, Magnetic Resonance Spectroscopy, Mercury, Protein Binding, Protein Conformation, Zinc},
	issn = {0006-291X},
	author = {Smith, R J and Bryant, R G}
}
