Synthesis and structural characterization of η6-arene-ruthenium(II) complexes of α-amino acids with coordinating side chains

1989 ◽  
Vol 377 (2-3) ◽  
pp. 357-366 ◽  
Author(s):  
W.S. Sheldrick ◽  
S. Heeb
2015 ◽  
Vol 39 (5) ◽  
pp. 3319-3326 ◽  
Author(s):  
Madhusudana M. B. Reddy ◽  
K. Basuroy ◽  
S. Chandrappa ◽  
B. Dinesh ◽  
B. Vasantha ◽  
...  

γn amino acid residues can be incorporated into structures in γn and hybrid sequences containing folded and extended α and δ residues.


Author(s):  
Jolanta Cieślak ◽  
Akimasa Miyanaga ◽  
Makoto Takaishi ◽  
Fumitaka Kudo ◽  
Tadashi Eguchi

Adenylation enzymes play an important role in the selective incorporation of the cognate carboxylate substrates in natural product biosynthesis. Here, the biochemical and structural characterization of the adenylation enzyme IdnL7, which is involved in the biosynthesis of the macrolactam polyketide antibiotic incednine, is reported. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mimic, 5′-O-[N-(L-alanyl)sulfamoyl]adenosine, was determined at 2.1 Å resolution. The structure of IdnL7 explains the broad substrate specificity of IdnL7 towards small L-amino acids.


2011 ◽  
Vol 17 (46) ◽  
pp. 12834-12834
Author(s):  
Sunil K. Pandey ◽  
Ganesh F. Jogdand ◽  
João C. A. Oliveira ◽  
Ricardo A. Mata ◽  
Pattuparambil R. Rajamohanan ◽  
...  

2012 ◽  
Vol 2012 (13) ◽  
pp. 2656-2663 ◽  
Author(s):  
Awadut G. Giri ◽  
Ganesh F. Jogdand ◽  
Pattuparampil R. Rajamohanan ◽  
Sunil K. Pandey ◽  
Chepuri V. Ramana

Author(s):  
Consiglia Tedesco ◽  
Eleonora Macedi ◽  
Alessandra Meli ◽  
Giovanni Pierri ◽  
Giorgio Della Sala ◽  
...  

The synthesis and the structural characterization of a cyclic hexapeptoid with four methoxyethyl and two propargyl side chains have disclosed the presence of a hydrate crystal form [form (I)] and an anhydrous crystal form [form (II)]. The relative amounts of form (I) and form (II) in the as-purified product were determined by Rietveld refinement and depend on the purification procedures. In crystal form (I), peptoid molecules assemble in a columnar arrangement by means of side-chain-to-backbone C=CH...OC hydrogen bonds. In the anhydrous crystal form (II), cyclopeptoid molecules form ribbons by means of backbone-to-backbone CH2...OC hydrogen bonds, thus mimicking β-sheet secondary structures in proteins. In both crystal forms side chains act as joints among the columns or the ribbons and contribute to the stability of the whole solid-state assembly. Water molecules in the hydrate crystal form (I) bridge columns of cyclic peptoid molecules, providing a more efficient packing.


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