The Journal of organic chemistry, 77(12), 5423-5428 (2012-05-24)
A short, concise synthesis of enantiopure, side chain-modified α-amino acids such as 4-oxo-L-norvaline, 6-oxo-L-homonorleucine, and 5-cis-alkyl prolines is described. Knoevenagel condensation of l-aminocarboxylate-derived β-ketoesters with aldehydes followed by reductive decarboxylation results in unnatural α-amino acids in good yield. A fluorescent
The journal of physical chemistry. B, 114(36), 11820-11826 (2010-08-24)
Following the studies of urea denaturation of β-hairpins using molecular dynamics, in this paper, molecular dynamics simulations of two peptides, a 35 residue three helix bundle villin headpiece protein HP-35 and its doubly norleucine-substituent mutant (Lys24Nle/Lys29Nle) HP-35 NleNle, were undertaken
Australian veterinary journal, 89(3), 95-100 (2011-02-18)
Four dogs presented with clinical signs of severe hepatic disease after consuming a commercial camel meat diet. Laboratory investigation revealed evidence of severe liver disease, including markedly increased serum alanine aminotransferase (ALT) activity and total bilirubin concentration, and prolonged clotting
Proceedings of the National Academy of Sciences of the United States of America, 111(1), 433-438 (2013-12-19)
Pathogenic microbes have evolved complex secretion systems to deliver virulence factors into host cells. Identification of these factors is critical for understanding the infection process. We report a powerful and versatile approach to the selective labeling and identification of secreted
Proceedings of the National Academy of Sciences of the United States of America, 108(15), 6103-6108 (2011-03-29)
Determining the rate of forming the truly folded conformation of ultrafast folding proteins is an important issue for both experiments and simulations. The double-norleucine mutant of the 35-residue villin subdomain is the focus of recent computer simulations with atomistic molecular
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