Predictable Conformational Diversity in Foldamers of Sugar Amino Acids

Systematic conformational search was carried out for monomers and homohexamers of furanoid β-amino acids: cis-(S,R) and trans-(S,S) stereoisomers of aminocyclopentane carboxylic acid (ACPC), two different aminofuranuronic-acids (AFU(alpha) and AFUβ), their isopropylidene derivatives (AFU(ip)) as well as the key intermediate β-aminotetrahydrofurancarboxylic acid (ATFC). Stereochemistry of the building blocks was chosen to match with that of natural sugar amino acid (xylose and ribose) precursors (XylAFU and RibAFU). Results show that hexamers of cis furanoid beta-amino acids show great variability: while hydrophobic cyclopentane (cis(ACPC)6), and hydrophilic (XylAFU(alpha)/(beta))6 foldamers favor two different zigzagged conformation as hexamers, the backbone fold turns into a helix in case of (cisATFC)6 (10-helix) and (XylAFU(ip))6 (14-helix). Trans stereochemistry resulted in hexamers exclusively of right-handed helix conformation, (H12P)6, regardless of their polarity. We found that the preferred oligomeric structure of XylAFU(alpha)/(beta) is conformationally compatible with beta-pleated sheets, while that of the trans/(S,S) units match with alpha-helices of proteins

Caracterización del proteoma del virus de mosaico del babaco

The babaco mosaic virus (BMV) was recently reported thanks to studies at the level of sequence, resulting in similarity with the Papaya mosaic virus. However, in this study we proceeded to determine the three-dimensional structural model and characterize the functions of BMV proteins (CP, RdRp, Helicase, Methyltransferase, AlkB, TGB1, TGB2 and TGB3). through the use of bioinformatics tools...El virus del mosaico babaco (VMB) fue recientemente reportado gracias a estudios realizados a nivel de secuencia permitiéndonos conocer la similitud que tiene con el virus del mosaico de la papaya. Sin embargo, no hay información sobre la similitud que hay a nivel de estructura, es por ello que en este estudio se procedió a determinar su modelo estructural tridimensional y caracterizar las funciones de las proteínas del VMB (CP, RdRp, Helicasa, Metiltransferasa, AlkB, TGB1, TGB2 y TGB3), mediante el uso de herramientas bioinformáticas..