Asymmetric syntheses of optically active .alpha.,.beta.-disubstituted .beta.-amino acids

1993 ◽  
Vol 58 (17) ◽  
pp. 4758-4763 ◽  
Author(s):  
Kevin Burgess ◽  
Lee T. Liu ◽  
Biman Pal
Keyword(s):  
Amino Acids ◽  
Optically Active ◽  
Asymmetric Syntheses ◽  
Alpha Beta

Asymmetric syntheses of optically active α-amino acids by hydrocyanic acid addition to the optically active Schiff base

1970 ◽  
Vol 48 (12) ◽  
pp. 1881-1884 ◽  
Author(s):  
Mahendra S. Patel ◽  
Michael Worsley
Keyword(s):  
Amino Acids ◽  
Schiff Base ◽  
Optical Purity ◽  
Optically Active ◽  
Hydrocyanic Acid ◽  
Asymmetric Syntheses ◽  
Acid Addition

The syntheses of L(+) and D(−) enantiomers of α-amino acids, norvaline, norleucine, and leucine, as their hydrochloride salts have been achieved in almost 100% optical purity and 40–60% overall yield.

scholarly journals The T Cell Receptor (TRB) Locus in Tursiops truncatus: From Sequence to Structure of the Alpha/Beta Heterodimer in the Human/Dolphin Comparison

Genes ◽  
2021 ◽  
Vol 12 (4) ◽  
pp. 571
Author(s):  
Giovanna Linguiti ◽  
Sofia Kossida ◽  
Ciro Leonardo Pierri ◽  
Joumana Jabado-Michaloud ◽  
Geraldine Folch ◽  
...  
Keyword(s):  
Amino Acids ◽  
T Cell ◽  
T Cell Receptor ◽  
Tursiops Truncatus ◽  
Cell Receptor ◽  
Sequence Alignments ◽  
T Cell Receptor Beta ◽  
Alpha Beta ◽  
Receptor Beta ◽  
Complementarity Determining Region

The bottlenose dolphin (Tursiops truncatus) belongs to the Cetartiodactyla and, similarly to other cetaceans, represents the most successful mammalian colonization of the aquatic environment. Here we report a genomic, evolutionary, and expression study of T. truncatus T cell receptor beta (TRB) genes. Although the organization of the dolphin TRB locus is similar to that of the other artiodactyl species, with three in tandem D-J-C clusters located at its 3′ end, its uniqueness is given by the reduction of the total length due essentially to the absence of duplications and to the deletions that have drastically reduced the number of the germline TRBV genes. We have analyzed the relevant mature transcripts from two subjects. The simultaneous availability of rearranged T cell receptor α (TRA) and TRB cDNA from the peripheral blood of one of the two specimens, and the human/dolphin amino acids multi-sequence alignments, allowed us to calculate the most likely interactions at the protein interface between the alpha/beta heterodimer in complex with major histocompatibility class I (MH1) protein. Interacting amino acids located in the complementarity-determining region according to IMGT numbering (CDR-IMGT) of the dolphin variable V-alpha and beta domains were identified. According to comparative modelization, the atom pair contact sites analysis between the human MH1 grove (G) domains and the T cell receptor (TR) V domains confirms conservation of the structure of the dolphin TR/pMH.

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