scholarly journals A Novel Recombinant Fusion Protein Encoding a 20-Amino Acid Residue of the Third Extracellular (E3) Domain of CCR2 Neutralizes the Biological Activity of CCL2

2009 ◽  
Vol 183 (1) ◽  
pp. 732-739 ◽  
Author(s):  
Liat Izhak ◽  
Gizi Wildbaum ◽  
Yaniv Zohar ◽  
Rachel Anunu ◽  
Leah Klapper ◽  
...  
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Fusion Protein ◽  
Amino Acid Residue ◽  
Recombinant Fusion Protein ◽  
The Third ◽  
Protein Encoding

Haplotypic diversity of DQA1*03 and *05 subtypes differing at amino acid residue 160 encoded in the third exon in 2215 Japanese individuals

1997 ◽  
Vol 49 (1) ◽  
pp. 46-52 ◽  
Author(s):  
T. Kaneshige ◽  
M. Hashimoto ◽  
T. Kinoshita ◽  
T. Moribe ◽  
A. Inagawa ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
The Third ◽  
Haplotypic Diversity

The importance of the B10 amino acid residue to the biological activity of insulin. [Lys10-B] human insulin

1982 ◽  
Vol 1 (3) ◽  
pp. 177-189 ◽  
Author(s):  
Gerald Schwartz ◽  
G. Thompson Burke ◽  
Panayotis G. Katsoyannis
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Human Insulin ◽  
Amino Acid Residue

Critical role of the A2 amino acid residue in the biological activity of insulin: [2-glycine-A]- and [2-alanine-A]insulins

Biochemistry ◽  
1984 ◽  
Vol 23 (7) ◽  
pp. 1405-1413 ◽  
Author(s):  
Kouki Kitagawa ◽  
Hiroshi Ogawa ◽  
G. Thompson Burke ◽  
Jacob D. Chanley ◽  
Panayotis G. Katsoyannis
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Residue ◽  
Critical Role

The amino acid residue at position 95 and the third CDR region in the H chain determine the ceiling affinity and the maturation pathway of an anti-(4-hydroxy-3-nitrophenyl)acetyl antibody

2010 ◽  
Vol 48 (1-3) ◽  
pp. 48-58 ◽  
Author(s):  
Akikazu Murakami ◽  
Yuka Takahashi ◽  
Miyuki Nishimura ◽  
Takeyuki Shimizu ◽  
Takachika Azuma
Keyword(s):  
Amino Acid ◽  
Amino Acid Residue ◽  
The Third

scholarly journals The mitochondrial genome of the honeybee Apis mellifera: complete sequence and genome organization.

Genetics ◽  
1993 ◽  
Vol 133 (1) ◽  
pp. 97-117 ◽  
Author(s):  
R H Crozier ◽  
Y C Crozier
Keyword(s):  
Amino Acids ◽  
Apis Mellifera ◽  
Amino Acid ◽  
Base Composition ◽  
Complete Sequence ◽  
The Third ◽  
Protein Encoding ◽  
Codon Positions ◽  
Encoding Genes ◽  
Codon Family

Abstract The complete sequence of honeybee (Apis mellifera) mitochondrial DNA is reported being 16,343 bp long in the strain sequenced. Relative to their positions in the Drosophila map, 11 of the tRNA genes are in altered positions, but the other genes and regions are in the same relative positions. Comparisons of the predicted protein sequences indicate that the honeybee mitochondrial genetic code is the same as that for Drosophila; but the anticodons of two tRNAs differ between these two insects. The base composition shows extreme bias, being 84.9% AT (cf. 78.6% in Drosophila yakuba). In protein-encoding genes, the AT bias is strongest at the third codon positions (which in some cases lack guanines altogether), and least in second codon positions. Multiple stepwise regression analysis of the predicted products of the protein-encoding genes shows a significant association between the numbers of occurrences of amino acids and %T in codon family, but not with the number of codons per codon family or other parameters associated with codon family base composition. Differences in amino acid abundances are apparent between the predicted Apis and Drosophila proteins, with a relative abundance in the Apis proteins of lysine and a relative deficiency of alanine. Drosophila alanine residues are as often replaced by serine as conserved in Apis. The differences in abundances between Drosophila and Apis are associated with %AT in the codon families, and the degree of divergence in amino acid composition between proteins correlates with the divergence in %AT at the second codon positions. Overall, transversions are about twice as abundant as transitions when comparing Drosophila and Apis protein-encoding genes, but this ratio varies between codon positions. Marked excesses of transitions over chance expectation are seen for the third positions of protein-coding genes and for the gene for the small subunit of ribosomal RNA. For the third codon positions the excess of transitions is adequately explained as due to the restriction of observable substitutions to transitions for conserved amino acids with two-codon families; the excess of transitions over expectation for the small ribosomal subunit suggests that the conservation of nucleotide size is favored by selection.

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