Asymmetric hydrogenations of α-enamides using Burk's DuPHOS-based Rh(I) catalysts generated high enantiomerically pure α-amino acid derivatives, which subsequently underwent Suzuki cross couplings with boronic acid derivatives to afford these aromatic substituted amino acids in high yields and with high enantioselectivity. Amino acid being organic compound molecules can form various different links with each other due to the versatile nature of carbon.This enables the great diversity of proteins that can be found in nature.These are an essential nutrient in our diet. These amino acids bond together to form a larger protein molecule. Asymmetric hydrogenations of α-enamides using Burk's DuPHOS-based Rh(I) catalysts generated high enantiomerically pure α-amino acid derivatives, which subsequently underwent Suzuki cross couplings with boronic acid derivatives to afford these aromatic substituted amino acids in high yields and with high enantioselectivity.ĪB - A series of novel hydrophobic, bulky χ2-constrained phenylalanine and naphthylalanine derivatives were designed and synthesized. There are some 20 amino acids in the proteins that we consume. N2 - A series of novel hydrophobic, bulky χ2-constrained phenylalanine and naphthylalanine derivatives were designed and synthesized. The views expressed are those of the authors and not necessary those of the USPHS. To exclude the influence of mutation-induced improper folding on enzyme activity, the oligomerization state and thermal unfolding of the isolated and purified mutants were compared with those of the wt- Pc PAL. b SDS-PAGE analysis of Tvn1315 and N-terminally truncated proteins expressed in E. Hydrophobic binding pocket residues in boxes were exchanged individually or in combination with smaller hydrophobic amino acids V or A. The numbers represent the amino acid residue numbers (cf Sakaguchi et al. Ming Yan for the use of their chiral HPLC column and assistance. N-terminal amino acid sequences (a) and SDS-PAGE analysis (b) of Tvn1315 and N-terminally truncated proteins.a N-terminal amino acid sequences of Tvn1315, Tvn13155, Tvn131510, and Tvn131520. McGrath for the use of his group's polarimeter and Professor Michael P. This work is supported by US Public Health Service (DK 17420) and the National Institute of Drug Abuse (DA 06284). T1 - Design and synthesis of hydrophobic, bulky χ2-constrained phenylalanine and naphthylalanine derivatives

Bulky hydrophobic amino acids