ArticleInternational journal of biochemistry and biophysics2021
Signature of Glycylglutamic Acid Structure.
Article in International journal of biochemistry and biophysics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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1 citing paper in PubMed, 2 citations in OpenAlex.
- Molecular dynamics of fibric acids.European journal of chemistry (Print) · 2022Article
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
Abstract
backgroundGlutamate (Glu) is of great interest in biomedical research. It is considered a biomarker in diabetes, which may potentially contribute to the development of autism in genetically vulnerable human populations, and it is found in relation to advanced glycation end products (AGEs) [1]. Additionally, Glu plays an active role in the function of ligand-gated ion channel glutamate receptors, chloride channels capable of filtering glutamate, as well as Potassium (K
objectivesThe current study was undertaken to understand the signal patterns of Cβ-CH MATERIALS AND
methodsNMR spectra of GlyGlu were measured in D
resultsThe sidechain of Glu in the dipeptide dissimilates the β form. The amino group of Gly (Glycine) is protonated and exhibits hydrogen bonding with the main chain carboxylate group of a symmetry-related Glu that is deprotonated in the crystal packing of GlyGlu. The deprotonated main chain carboxylate of Glu is also in hydrogen-bonding distance from the side chain carboxylic acid group that is in the protonated form of a symmetry-related Glu of the dipeptide. The Cβ-CH
conclusionThe results reported will be useful for monitoring changes that Glu and/or molecules in connection to Glu may undergo in
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