Examples of phenylalanine

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There is a selective increase in the branched chain amino acids, phenylalanine and alanine.
The rat a7 subunit has a phenylalanine and an aromatic ring structure.
This indicates that upon irradiation phenylalanine is little affected or undergoes only some chemical transformation, depending on the dose.
A total of 29 species were detected, most corresponding to products with higher molecular weight than phenylalanine, including tyrosine.
This knowledge gave researchers the means (dietary restriction of phenylalanine intake) and the critical time (ideally the first postnatal month) for efficacious treatment.
The almost linear behaviour indicates that phenylalanine is still present at high doses to form products with larger absorption coefficients.
Conversely, the actual phenotypic disease of phenylketonuria showed increasingly incomplete penetrance with widespread introduction of low phenylalanine diet.
Thus, for instance, phenylalanine cations show a peak at 164.
Sequencing revealed phenylalanine at position 167 in all seven worms.
The degradation products partly maintain life-building capability, as phenylalanine still belongs to the protein amino acid set, and partly do not.
As well as competing with it for entry into the brain, phenylalanine also competes with tryptophan in the pathways of neurotransmitter synthesis.
They are symmetrically arranged and centred about two phenylalanine residues which presumably interact with the loop region of the hairpin pair.
Table 2 presents the percentage of the remaining phenylalanine after irradiation at different doses from the chromatographic analysis.
Phenylalanine was irradiated at a concentration of 2r10x2 mol lx1 and spectra were taken at a concentration of 1r10x2 mole lx1.
Cysteine may participate in the formation of bonds that stabilize the functional conformation of tuberin and substitution of bulky phenylalanine for relatively small cysteine may affect tuberin activity.
Benzimidazole resistance in parasitic nematodes has been linked to a single amino acid substitution (phenylalanine to tyrosine) at position 200 on the -tubulin molecule.
The pathological phenotypes are modified considerably by environmental factors like reducing the intake of phenylalanine in the diet (a fact which forms the basis for an alleviating treatment).

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