Shark Myelin Basic Protein: Amino Acid Sequence, Secondary Structure, and Self-Association

1. A procedure is described for the detection and assessment of informational complementarity in an amino acid sequence; it is based on possible autocomplementarity in the mRNA, and involves codon-to-codon matching. 2. This procedure was applied to myelin basic protein, a variety of protamines, histone IV, silk fibroin, rat skin collagen α1 chain and a sheep keratin. A multiplicity of extensive low-probability informational symmetries, based on codon-to-codon matching, were detected. 3. These low-probability orderings, which are independent of the actual mRNA codons, are rationalized in terms of the evolutionary ordering of the amino acid sequences concerned, in such a way that constraints on the secondary structure of the coding polynucleotides were satisfied. This possible interpretation is supported by a number of significant common properties of the protein sequences analysed.

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The bovine plasma retinol-binding protein. Amino acid sequence, interaction with transthyretin, crystallization and preliminary X-ray data

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1990.tb19254.x ◽

1990 ◽

Vol 192 (2) ◽

pp. 507-513 ◽

Cited By ~ 25

Author(s):

Rodolfo BERNI ◽

Monica STOPPINI ◽

Maria Carla ZAPPONI ◽

Maria Laura MELONI ◽

Hugo L. MONACO ◽

...

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Binding Protein ◽

Retinol Binding Protein ◽

Protein Amino Acid ◽

X Ray ◽

Protein Amino Acid Sequence ◽

Bovine Plasma ◽

Plasma Retinol

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The binding of calmodulin to myelin basic protein and histone H2B

Biochemical Journal ◽

10.1042/bj1890227 ◽

1980 ◽

Vol 189 (2) ◽

pp. 227-240 ◽

Cited By ~ 49

Author(s):

R J Grand ◽

S V Perry

Keyword(s):

Amino Acid ◽

Amino Acid Sequence ◽

Myelin Basic Protein ◽

Basic Protein ◽

Binding Protein ◽

Bovine Brain ◽

Sequence Determination ◽

Partial Amino Acid Sequence ◽

Histone H2b ◽

Calmodulin Binding

1. A calmodulin-binding protein of apparent mol.wt. 19 000 has been purified from chicken gizzard. Similar proteins have been isolated from bovine uterus, rabbit skeletal muscle and rabbit liver. 2. These proteins migrated as an equimolar complex with bovine brain calmodulin on electroporesis on polyacrylamide gels in the presence of Ca2+ and 6M-urea. The complex was dissociated in the presence of EGTA. 2. The chicken gizzard calmodulin-binding protein has been shown to be identical with chicken erythrocyte histone H2B on the basis of partial amino acid sequence determination. 4. The calmodulin-binding proteins of apparent mol.wt. 22 000 isolated previously from bovine brain [Grand & Perry (1979) Biochem. J. 183, 285-295] has been shown, on the basis of partial amino-acid-sequence determination, to be identical with myelin basic protein. 5. The activation of bovine brain phosphodiesterase by calmodulin is inhibited by excess bovine uterus calmodulin-binding protein (histone H2B). 6. The phosphorylation of myelin basic protein by phosphorylase kinase is partially inhibited, whereas the phosphorylation of uterus calmodulin-binding protein (histone H2B) is unaffected by calmodulin or troponin C. 7. The subcellular distribution of myelin basic protein and calmodulin suggests that the two proteins do not exist as a complex in vivo.

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