Signaling amino acids

The rate of protein synthesis, in liver and other tissues, which depends on the concentrations of some hormones and the concentration(s) of signal amino acids (e.g. leucine) (Figure 8.16). 

Additional information <11, 13> (<13>, STY protein contains a putative nuclear localization signal [23] <11>, nuclear localization of DYRKIA is mediated by its nuclear targeting signal, amino acids 105-139, but ist characteristic subnuclear distribution depends on additional N-terminal elements, amino acids 1-104 [15]) [15, 23]... 

Codon Sequence of three nucleotides that codes for a single amino acid (or a termination signal)... 

NMR signals of the amino acid ligand that are induced by the ring current of the diamine ligand" ". From the temperature dependence of the stability constants of a number of ternary palladium complexes involving dipeptides and aromatic amines, the arene - arene interaction enthalpies and entropies have been determined" ". It turned out that the interaction is generally enthalpy-driven and counteracted by entropy. Yamauchi et al. hold a charge transfer interaction responsible for this effect. 

Figure 18.16 One-dlmenslonal NMR spectra, (a) H-NMR spectrum of ethanol. The NMR signals (chemical shifts) for all the hydrogen atoms In this small molecule are clearly separated from each other. In this spectrum the signal from the CH3 protons Is split Into three peaks and that from the CH2 protons Into four peaks close to each other, due to the experimental conditions, (b) H-NMR spectrum of a small protein, the C-terminal domain of a cellulase, comprising 36 amino acid residues. The NMR signals from many individual hydrogen atoms overlap and peaks are obtained that comprise signals from many hydrogen atoms. (Courtesy of Per Kraulis, Uppsala, from data published in Kraulis et al.. Biochemistry 28 7241-7257, 1989.)...

These signals in the NOE spectra therefore in principle make it possible to determine which fingerprint in the COSY spectrum comes from a residue adjacent to the one previously identified. For example, in the case of the lac-repressor fragment the specific Ser residue that was identified from the COSY spectrum was shown in the NOE spectrum to interact with a His residue, which in turn interacted with a Val residue. Comparison with the known amino acid sequence revealed that the tripeptide Ser-His-Val occurred only once, for residues 28-30. 

The protein contains an N-terminal signal peptide of 17 amino acid residues for secretion. The luminescence reaction of coelenterazine catalyzed by the recombinant luciferase shows a luminescence emission maximum at 485 nm, whereas the luminescence catalyzed by the native luciferase shows a maximum at 480 nm. 

The ankyrin repeat motif is one of the most common protein-protein interaction domains. Ankyrin repeats are modules of about 33 amino acids repeated in tandem. They are found in a large number of proteins with diverse cellular functions such as transcriptional regulators, signal transducers, cell-cycle regulators, and cytoskeletal proteins. 

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