In protein structures, side-chains of asparagine and aspartic acid (Asx) and glutamine and glutamic acid (Glx) can approach their own backbone nitrogen or carbonyl group.
2008), showing that this amino acid must have some physico-chemical property important for protein structure (such as formation of asparagine ladders (Jenkins and Pickersgill 2001)) that is counterbalanced by its tendency to age.
Wilhelm, S.G. Lee, N.K. Kalyan, S.M. Cheng, F. Wiener, W. Pierzchala, P.P. Hung, Alterations in the domain structure of tissue-type plasminogen activator change the nature of asparagine glycosylation.
In the structural model of NcLPMO9C built using the crystal structure of NcLPMO9D (PDB 4EIR [ 44]), three asparagine residues exposed at the surface of NcLPMO9C were suggested to be involved in the interaction with oligosaccharides, constituting the +2 subsite [ 30].
Furthermore, analysis of the solution structure of S100A4 revealed three potentially unstable Asparagine residues N65, N68 and N87 with CD values of 8.293, 21.696 and 13.500, respectively, which suggests that these residues could be subject to deamidation.
The side chains of asparagine at position 9 form hydrogen bonds in the loop structure [ 6].
Results of total amount of asparagine and glutamine (a) and ratio of asparagine to glutamine (b) in feed media were listed.
DFT optimization of asparagine resulted in 10 stable conformations with ∆EDFT < 10 kJ.mol− 1.
The adsorption of asparagine (Asn) on a gold electrode from 0.1 M LiClO4 aqueous solutions was investigated.
Fig. 4 Expression levels of OsASs and contents of asparagine and NH4+ in the basal portions.
