Amino-acid residues glutamine

Later analyses of calfskin collagen show two additional amino acid residues, glutamine and asparagine, each present in about 2% concentration (by number of residues). The distinctive groups have been added to the table. 

It is a peptide containing 27 amino acid residues containing the amino acids L-histidine (His) L-aspartic acid (Asp) L-serine (Ser) glycine (Gly) L-threonine (Thr) L-phenyl-alanine (Phe) L-glutamic acid (Glu) L-glutamine [Glu(NHj)] L-leucine (Leu) L-arginine (Arg) L-alanine (Ala) and L-valinamide (Va -NHj). 

The tertiary structure of glutamate racemase has already been resolved and it has also been shown that a substrate analog glutamine binds between two cysteine residues. These data enabled us to predict that the new proton-donating amino acid residue should be introduced at position 74 instead of Gly for the inversion of enantioselectivity of the decarboxylation reaction. 

RIBULOSE-5-PHOSPHATE 3-EPIM ERASE Escherichia coll glutamine synthetase, ENZYME CASCADE KINETICS GLUTAMINE SYNTHETASE Essential amino acid residues in catalysis, AFFINITY LABELING ESTERASES... 

In addition to the amino acids described above, several other amino acid residues are also reactive toward compounds containing heavy atoms. These are the side chains of arginine, asparagine, glutamine, lysine, tryptophan, and tyrosine. Those that are not reactive are alanine, glycine, isoleucine. 

In addition to structural domains devoted to DNA binding and dimerization (or oligomerization), many regulatory proteins must interact with RNA polymerase, with unrelated regulatory proteins, or with both. At least three different types of additional domains for protein-protein interaction have been characterized (primarily in eukaryotes) glutamine-rich, proline-rich, and acidic domains, the names reflecting the amino acid residues that are especially abundant. 

GGGCGG), is usually quite near the TATA box. The DNA-binding domain of the Spl protein is near its carboxyl terminus and contains three zinc fingers. Two other domains in Spl function in activation, and are notable in that 25% of their amino acid residues are Gin. A wide variety of other activator proteins also have these glutamine-rich domains. 

Of the following amino acid residues—methionine, histidine, arginine, phenylalanine, valine, glutamine, glutamic acid—which would you expect to find on the (a) surface of a protein and which would you expect to find (b) in the interior ... 

Approximately 150 different amino acid residues have been reported in proteins (1 5). At least half of these could undergo chemical deteriorations under the conditions of stress usually encountered. Many of these deteriorative reactions involve hydrolytic scissions, not only of peptide bonds but of the many different nonprotein substances added covalently to proteins postribosomally. These susceptible side chain groups are indole, phenoxy, thioether, amino, imidazole, sulfhydryl, and derivatives of serine and threonine (such as 0-glycosyl or O-phosphoryl), the disulfides of cystine, and, of course, the amides (such as asparagine and glutamine). With strong acid or alkali, other residues, such as serine and threonine, also are less stable. 

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