Results 41 to 50 of about 212,752 (309)

Controlled self-assembly of modified aromatic amino acids

open access: yes, 2021
We report the self-assembly of carbobenzoxyphenylalanine (Z-Phe-OH), carbobenzoxytryptophan (Z-Trp-OH), carbobenzoxytyrosine (Z-Tyr-OH) and N-(9-Fluorenylmethoxycarbonyl)-O-tert-butyl-L-tyrosine (Fmoc-Tyr(tbu)-OH) to well-defined morphologies such as ...
Bharti , Koshti   +4 more
core   +1 more source

Evaluation of aromatic amino acids as potential biomarkers in breast cancer by Raman spectroscopy analysis

open access: yesScientific Reports, 2021
The scope of the work undertaken in this paper was to explore the feasibility and reliability of using the Raman signature of aromatic amino acids as a marker in the detection of the presence of breast cancer and perhaps, even the prediction of cancer ...
Shaymus Contorno   +2 more
doaj   +1 more source

Tyrosine, Phenylalanine, and Tryptophan Undergo Self-Aggregation in Similar and Different Manners

open access: yesAtmosphere, 2022
Phenylalanine, tyrosine, and tryptophan are aromatic amino acids, and they are of high interest in both health science and biotechnology. These amino acids form organized structures, like fibrils and nanotubes.
Sahin Uyaver
doaj   +1 more source

4 Aromatic Amino Acids in the Brain

open access: yes, 2007
This chapter describes the aromatic l-amino acids tryptophan and tyrosine and the effects on tyrosine metabolism of phenylalanine. Tryptophan and phenylalanine are essential amino acids and must ultimately be derived from dietary proteins; tyrosine is ...
M. Cansev   +3 more
core   +1 more source

Interaction of Aromatic Amino Acids with Neutral Polyadenylic Acid [PDF]

open access: yesProceedings of the National Academy of Sciences, 1971
The aromatic amino acids tryptophan, phenylalanine, and histidine interact with singlestranded polyadenylic acid [poly(A)] as observed by proton magnetic resonance spectroscopy. The chemical shift of the C 2 and C 8 protons of the adenine moiety of poly(A) is consistent with a destacking of ...
M, Raszka, M, Mandel
openaire   +2 more sources

Neutrophils as a source of branched-chain, aromatic and positively charged free amino acids

open access: yesCell Adhesion & Migration, 2019
Neutrophils release branched-chain (valine, isoleucine, leucine), aromatic (tyrosine, phenylalanine) and positively charged free amino acids (arginine, ornithine, lysine, hydroxylysine, histidine) when adhere and spread onto fibronectin.
Svetlana I. Galkina   +5 more
doaj   +1 more source

Metabolism of Tryptophan in the Liver: Interference with Decarboxylation of Other Aromatic Amino Acids

open access: yesActa Medica, 2000
Decarboxylation of aromatic amino acid in mammalian tissues is catalyzed by aromatic amino acid decarboxylase (EC. 4.1.1.28, AAD). The enzyme differs in its affinity to individual aromatic amino acids, the best substrates being 3,4-dihydroxyphenylalanine
Jaroslav Dršata, Eliška Marklová
doaj   +1 more source

Plasma Amino Acid Concentrations Predict Mortality in Patients with End-Stage Liver Disease. [PDF]

open access: yesPLoS ONE, 2016
The liver plays a key role in amino acid metabolism. In former studies, a ratio between branched-chain and aromatic amino acids (Fischer's ratio) revealed associations with hepatic encephalopathy.
Benedict Kinny-Köster   +6 more
doaj   +1 more source

Direct synthesis of α-thio aromatic acids from aromatic amino acids [PDF]

open access: yesTetrahedron Letters, 2018
Modified amino acids are useful synthetic components in both chemistry and biology. Here we describe a simple, scalable two-step procedure to generate α-thio aromatic acids from aromatic amino acids with yields of up to 96%. Diazotization and α-lactone mediated bromination efficiently form the α-bromo acid with retention of configuration.
Eric R, Samuels, Irina, Sevrioukova
openaire   +2 more sources

Phase-separation propensity of non-ionic amino acids in peptide-based complex coacervation systems

open access: yes, 2022
Uncovering the sequence-encoded molecular grammar that governs the liquid–liquid phase separation (LLPS) of proteins is a crucial issue to understand dynamic compartmentalization in living cells and the emergence of protocells. Here, we present a model
Kentaro, Shiraki   +6 more
core   +1 more source

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