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Leucine following alanine-valine

The authors of this review have developed a somewhat different approach (3a) to the reading frame problem and feel that it imparts greater sensitivity. The technique is based on the assumption (which is borne out by statistics) that proteins express biases in the consecutive selection of amino acids within their primary structures. For instance, consider the hypothetical protein sequence [AVLITMA] in single letter code. It is assumed that valine follows alanine because proteins in general prefer valine after alanine, and then leucine preferentially follows alanine-valine for structural and/or functional reasons, and so forth. If these preferences (say for all amino acid trimers) can be found, then they should be useful in delineating reading... [Pg.23]

The Silurian Wills Creek, Tonoloway and Keyser Formations were tested for residual amino acids (Table V). The following were found cystine( ), histidine(P), arginine, glycine(P), aspartic acid(P), glutamic acid(P), threonine, alanine, valine, leucine. [Pg.18]

The properties of polypeptides and proteins are determined to a large extent by the chemistry of the side chain groups, which may be summarized briefly as follows. Glycine in a peptide permits a maximum of conformational mobility. The nine relatively nonpolar amino acids-alanine, valine, leucine, isoleucine, proline, methionine, phenylalanine, tyrosine, and tryptophan-serve as building blocks of characteristic shape. Tyrosine and tryptophan also participate in hydrogen bonding and in aromatic aromatic interactions within proteins. [Pg.54]

Table 5.2 lists the amino acid molar ratios determined for LHCP from several plant sources, and compares these results with the mean values obtained for the main glycopeptide subfraction (peak I in Table 5.1) from microbubble surfactant. It can be seen from Table 5.2 that the amino acid composition of LHCP clearly resembles that of the main glycopeptide subfraction. Specifically, in both cases nonpolar residues represent a majority and near constant fraction (i.e., 59-62%) of the amino acid composition, with the relative amounts of such residues in practically all individual cases listed following the pattern glycine > leucine, alanine, valine, proline > isoleucine, phenylalanine > methionine, tryptophan (Table 5.2). Accordingly, the glycopeptide fraction of microbubble surfactant may represent a degradation product of the light-harvesting chlorophyll a/b-protein, which is well known (ref. 373-375) to be extremely widely distributed in terrestrial, freshwater, and salt-water environments (cf. ref. 379). Table 5.2 lists the amino acid molar ratios determined for LHCP from several plant sources, and compares these results with the mean values obtained for the main glycopeptide subfraction (peak I in Table 5.1) from microbubble surfactant. It can be seen from Table 5.2 that the amino acid composition of LHCP clearly resembles that of the main glycopeptide subfraction. Specifically, in both cases nonpolar residues represent a majority and near constant fraction (i.e., 59-62%) of the amino acid composition, with the relative amounts of such residues in practically all individual cases listed following the pattern glycine > leucine, alanine, valine, proline > isoleucine, phenylalanine > methionine, tryptophan (Table 5.2). Accordingly, the glycopeptide fraction of microbubble surfactant may represent a degradation product of the light-harvesting chlorophyll a/b-protein, which is well known (ref. 373-375) to be extremely widely distributed in terrestrial, freshwater, and salt-water environments (cf. ref. 379).
More than 300 compounds had been identified in cocoa volatiles, 10% of which were carbonyl compounds (59,60). Acetaldehyde, 2-methylpropanal, 3-methylbutanal, 2-methylbutanal, phenylacetaldhyde and propanal were products of Strecker degradation of alanine, valine, leucine, isoleucine, phenyl-acetaldehyde, and a-aminobutyric acid, respectively. Eckey (61) reported that raw cocoa beans contain about 50-55% fats, which consisted of palmitic (26.2%), stearic (34.4%), oleic (37.3%), and linoleic (2.1%) acids. During roasting cocoa beans these acids were oxidized and the following carbonyl compounds might be produced - oleic 2-propenal, butanal, valeraldehyde, hexanal, heptanal, octanal, nonanal, decanal, and 2-alkenals of Cg to C-q. Linoleic ethanal, propanal, pentanal, hexanal, 2-alkenals of to C q, 2,4-alkadienals of Cg to C-q, methyl ethyl ketone and hexen-1,6-dial. Carbonyl compounds play a major role in the formation of cocoa flavor components. [Pg.226]

Problem 36.10 Various amino acids have been made in the following ways Direct ammonolysis glycine, alanine, valine, leucine, aspartic acid Gabriel synthesis glycine, leucine Malonic ester synthesis valine, isoleucine... [Pg.1140]

Activity was detected in the following amino-acids serine, aspartic acid, glutamic acid, lysine, histidine, arginine, alanine, valine, phenylalanine, and leucine... [Pg.158]

This pathway is followed by alanine, valine, isoleucine, and leucine. The prototype for all is the metabolism of alanine, which goes to activated acetate (acetyl-CoA) in two steps. Acetyl-CoA, of course, then can undergo a multitude of reactions. The first step is transamination, yielding in the usual manner the a-keto... [Pg.159]

On complete hydrolysis, a polypeptide gives two alanine, one leucine, one methionine, one phenylalanine, and one valine residue. Partial hydrolysis gives the following fragments Ala-Phe, Leu-Met, Val-Ala, Phe-Leu. It is known that the first amino acid in the sequence is valine and the last one is methionine. What is the complete sequence of amino acids ... [Pg.632]


See other pages where Leucine following alanine-valine is mentioned: [Pg.339]    [Pg.97]    [Pg.134]    [Pg.570]    [Pg.1199]    [Pg.136]    [Pg.476]    [Pg.126]    [Pg.303]    [Pg.453]    [Pg.71]    [Pg.361]    [Pg.177]    [Pg.2849]    [Pg.318]    [Pg.91]    [Pg.13]    [Pg.127]    [Pg.386]    [Pg.416]    [Pg.17]    [Pg.539]    [Pg.126]    [Pg.990]    [Pg.290]    [Pg.20]    [Pg.68]    [Pg.7]    [Pg.26]    [Pg.97]    [Pg.27]    [Pg.227]    [Pg.269]    [Pg.244]    [Pg.244]    [Pg.150]    [Pg.990]    [Pg.171]    [Pg.405]   
See also in sourсe #XX -- [ Pg.23 ]




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