Examples of aspartic

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The amino acids were: arginine (basic), tryptophan (neutral and hydrophobic), valine (neutral and hydrophobic) and aspartic acid (acidic).
Sequences of several aspartic proteinases from different plants are now available although the localization of the enzyme is not known in all cases.
We found a 1.9 kb aspartic proteinase message in dry seeds and seed pods.
Comparative modelling and analysis of amino acid substitutions suggests that the family of pregnancy-associated glycoproteins includes both active and inactive aspartic proteinases.
All members of this family share some sequence similarity and all are phosphorylated at a conserved aspartic acid residue.
These could represent incompletely processed forms of this enzyme which may not be active aspartic proteinase.
There are five major categories o f endopeptidases that might play a role in angiogenesis: cysteine, aspartic, serine, metalloand threonine proteases.
Aspartic proteinases in other plants have been shown to be tissue specific.
Based on the results in this study, candidate inhibitors include those from soybean, as well as proteinaceous inhibitors of aspartic and cysteine proteinases.
These results show that most alkylamino acids, as well as aspartic acid, can be polymerized in molten urea.
Localization of this protein and determination of its protease activity will expand our understanding of the role of these sequences in the plant aspartic proteinases.
It appears that each plant may regulate aspartic proteinase gene expression slightly differently.
Effect of different donor cells on embryo development and gene expression members of the aspartic proteinase gene family expressed in trophectoderm.
The presence of an aspartic acid in position 82, which is highly conserved among higher eukaryotes, is noted.
Vibrational spectroscopy of bacteriorhodopsin mutants : light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212.
Hookworm larvae also secrete aspartic protease activity that is capable of digesting skin macromolecules.
Cysteine and aspartic proteinase inhibitors had little effect (#16% inhibition) on the hydrolysis of both serine fluorogenic substrates.
Also, aspartic acid was found to polymerize in molten urea at a lower temperature than that at which aspartic acid alone had previously been thermally polymerized.
Although aspartic acid may be polymerized in the molten state by single heating, the reaction temperature in the molten urea was lower than that of self-polymerization.

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