The Histidine and Methionine Sequences of Rabbit Skeletal Tropomyosin

1972 ◽  
Vol 50 (3) ◽  
pp. 312-329 ◽  
Author(s):  
R. S. Hodges ◽  
L. B. Smillie
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Coiled Coil ◽  
Sequence Information ◽  
Chain Packing ◽  
Hydrophobic Residues ◽  
Coil Structure ◽  
Methionine Residues ◽  
Polypeptide Chains

Amino acid analyses of tropomyosin have previously shown four histidine and 13–14 methionine residues per mole (70 000 daltons) of tropomyosin. The isolation of two unique histidyl and five unique methionyl sequences is described. The number of unique methionyl peptides will undoubtedly be increased when more extensive sequence information becomes available although the value of 2 for the unique histidine sequences is considered to be a maximal one. These data support the conclusion that the two subunits of tropomyosin are similar in amino acid sequence. Both the acetylated NH2-terminal and COOH-terminal sequences of the protein have been determined in this study. The isolation and sequence analysis of two varieties of peptides arising from the COOH-terminus of the protein indicates either a degree of proteolysis during its isolation or a difference in the constituent polypeptide chains of tropomyosin in this region of their structures. The limited sequences reported indicate a repeat of hydrophobic residues as required by the inter-chain packing of a coiled-coil structure.

Cysteine Sequences of Rabbit Skeletal Tropomyosin

1972 ◽  
Vol 50 (3) ◽  
pp. 330-343 ◽  
Author(s):  
R. S. Hodges ◽  
L. B. Smillie
Keyword(s):  
Amino Acid ◽  
Acid Hydrolysis ◽  
Coiled Coil ◽  
Iodoacetic Acid ◽  
Amino Acid Sequences ◽  
Cysteic Acid ◽  
Chain Packing ◽  
Hydrophobic Residues ◽  
Coil Structure ◽  
Cysteine Content

Amino acid analyses of tropomyosin have shown three cysteine residues per mole (M.W. 70 000) of tropomyosin. The cysteine content was determined by cysteic acid determinations, incorporation of 14C-labelled iodoacetic acid into the protein, and the analysis of S-carboxymethylcysteine after acid hydrolysis. The isolation of three unique cysteinyl peptides is incompatible with a homogeneous tropomyosin preparation of two chemically identical subunits. The amino acid sequences reported in this study indicate a regular repeat of hydrophobic residues as required by the inter-chain packing of a coiled-coil structure.

Cyanogen Bromide Fragments of Rabbit Skeletal Tropomyosin

1973 ◽  
Vol 51 (1) ◽  
pp. 56-70 ◽  
Author(s):  
R. S. Hodges ◽  
L. B. Smillie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Coiled Coil ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Coil Structure ◽  
Polypeptide Chains

Previous studies have demonstrated that rabbit skeletal tropomyosin consists of two or more chemically non-identical but highly homologous polypeptide chains. Attempts by a variety of techniques to prepare pure tropomyosin chains in amounts adequate for chemical characterization have been unsuccessful to date. To provide more extensive information for the purpose of elucidating the relationship between amino acid sequence and the coiled-coil structure of tropomyosin, a cyanogen bromide treatment of the S-carboxymethylated protein was carried out. The fragments were separated into small and large components by gel filtration on Sephadex G-50. The small fragments were fractionated by ion-exchange chromatography and electrophoresis on paper and their sequences elucidated by conventional methods. Coupled with previous data, these results indicate a minimum of seven unique methionine sequences and are consistent with a high degree of homology in the tropomyosin polypeptide chains. From the mixture of the larger cyanogen bromide polypeptides, a fragment was isolated by ion-exchange chromatography on QAE-Sephadex. In aqueous buffer it had a molecular weight of 35 000 and an α-helical content of about 60% as estimated by circular dichroism. In 8 M urea its molecular weight was reduced to 15 000, a value in reasonable agreement with a minimal molecular weight of 17 000 calculated from its amino acid composition. From its histidine content (two residues) and the known COOH-terminal amino acid sequence of the protein, the fragment was concluded to be derived from the COOH-terminal half of the molecule. These results are consistent with a degree of 'coiled-coil' structure in a fragment representing about one-half of the tropomyosin molecule.

scholarly journals Partial amino acid sequence of rat pre-prolactin

1977 ◽  
Vol 161 (1) ◽  
pp. 189-192 ◽  
Author(s):  
R A Maurer ◽  
J Gorski ◽  
D J McKean
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Cysteine Residue ◽  
Amino Acid Residues ◽  
Partial Amino Acid Sequence ◽  
Considerable Similarity ◽  
Rat Pituitary ◽  
N Terminus ◽  
Methionine Residues

Rat pituitary mRNA was used to direct the cell-free synthesis of pre-prolactin labelled with [4,5-3H]leucine and either [35S] methioninc or [35S] cystine. Sequence analysis of the labelled protein indicates that pre-prolactin has 29 amino acid residues joined to the N-terminus of the prolactin sequence. Leucine residues were found at positions 13, 14, 15, 16, 21 and 22, methionine residues at positions 1, 17 and 18, and a cysteine residue at position 24 of the precursor sequence, and this partial sequence shows considerable similarity with other precursors that have been sequenced.

scholarly journals Amino-Acid Sequence of Rabbit Skeletal Tropomyosin and Its Coiled-Coil Structure

1972 ◽  
Vol 69 (12) ◽  
pp. 3800-3804 ◽  
Author(s):  
J. Sodek ◽  
R. S. Hodges ◽  
L. B. Smillie ◽  
L. Jurasek
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Coiled Coil ◽  
Coil Structure

Tropomyosin: Amino Acid Sequence and Coiled-Coil Structure

1973 ◽  
Vol 37 (0) ◽  
pp. 299-310 ◽  
Author(s):  
R. S. Hodges ◽  
J. Sodek ◽  
L. B. Smillie ◽  
L. Jurasek
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Coiled Coil ◽  
Coil Structure

scholarly journals Secondary structure of component 8c-1 of α-keratin. An analysis of the amino acid sequence

1986 ◽  
Vol 236 (3) ◽  
pp. 705-712 ◽  
Author(s):  
L M Dowling ◽  
W G Crewther ◽  
D A Parry
Keyword(s):  
Amino Acid ◽  
Secondary Structure ◽  
Amino Acid Sequence ◽  
Intermediate Filament ◽  
Coiled Coil ◽  
Terminal Region ◽  
Striking Similarity ◽  
Intermediate Filament Proteins ◽  
Coil Structure ◽  
Alpha Keratin

The amino acid sequence of component 8c-1 from alpha-keratin was analysed by using secondary-structure prediction techniques, homology search methods, fast Fourier-transform techniques to detect regularities in the linear disposition of amino acids, interaction counts to assess possible modes of chain aggregation and assessment of hydrophilicity distribution. The analyses show the following. The molecule has two lengths of coiled-coil structure, each about 20 nm long, one from residues 56-202 with a discontinuity from about residue 91 to residue 101, and the other from residues 219-366 with discontinuities from about residue 238 to residue 245 and at about residue 306. The acidic and basic residues in the coiled-coil segment between residues 102 and 202 show a 9,4-residue structural period in their linear disposition, whereas between residues 246 and 366 a period of 9.9 residues is observed in the positioning of ionic residues. Acidic and basic residues are out of phase by 180 degrees. Similar repeats occur in corresponding regions of other intermediate-filament proteins. The overall mean values for the repeats are 9.55 residues in the N-terminal region and 9.85 residues in the C-terminal region. The regions at each end of the protein chain (residues 1-55 and 367-412) are not alpha-helical and contain many potential beta-bends. The regions specified in have a significant degree of homology mainly due to a semi-regular disposition of proline and half-cystine residues on a three-residue grid; this is especially apparent in the C-terminal segment, in which short (Pro-Cys-Xaa)n regions occur. The coiled-coil segments of component 8c-1 bear a striking similarity to corresponding segments of other intermediate-filament proteins as regards sequence homology, structural periodicity of ionic residues and secondary/tertiary-structure predictions. The assessments of the probabilities that these homologies occurred by chance indicate that there are two populations of keratin filament proteins. The non-coiled-coil regions at each end of the chain are less hydrophilic than the coiled-coil regions. Ionic interactions between the heptad regions of components 8c-1 and 7c from the microfibrils of alpha-keratin are optimized when a coiled-coil structure is formed with the heptad regions of the constituent chains both parallel and in register.

Amino acid sequence of cyanogen bromide fragment CB3 of hog pepsin

1981 ◽  
Vol 46 (3) ◽  
pp. 655-666
Author(s):  
Ladislav Morávek ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Methionine Residues ◽  
Cyanogen Bromide Fragment

On the basis of the knowlidge of thermolytic, chymotryptic and substilisin peptides the amino acid sequence was determined of cyanogen bromide fragment CB3 representing the region between methionine residues I and II of pepsin: Thr-Gly-Ile-Leu-Gly-Tyr-Asp-Thr-Val-Gln-Val-Gly-Gly-Ile-Ser-Asp-Thr-Asn-Gln-Ile-Phe-Gly-Leu-Ser-Glu-Thr-Glu-Pro-Gly-Ser-Phe-Leu-Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu-Gly-Leu-Ala-Tyr-Pro-Ser-Ile-Ser-Ala-Ser-Gly-Ala-Thr-Pro-Val-Phe-Asp-Asn-Leu-Trp-Asp-Gln-Gly-Leu-Val-Ser-Gln-Asp-Leu-Phe-Ser-Val-Tyr-Leu-Ser-Ser-Asn-Asp-Asp-Ser-Gly-Ser-Val-Val-Leu-Leu-Gly-Gly-Ile-Asp-Ser-Ser-Tyr-Tyr-Thr-Gly-Ser-Leu-Asn-Trp-Val-Pro-Val-Ser-Val-Glu-Gly-Tyr-Trp-Gln-Ile-Thr-Leu-Asp-Ser-Ile-Thr-Met.

Identification of the gene encoding 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase in Burkholderia sp. HME13

2020 ◽  
Vol 85 (3) ◽  
pp. 626-629
Author(s):  
Hisashi Muramatsu ◽  
Hiroki Maguchi ◽  
Taisuke Harada ◽  
Takehiro Kashiwagi ◽  
Chul-Sa Kim ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Propionic Acid ◽  
Unknown Function ◽  
Protein Family ◽  
Amino Acid Sequence Analysis ◽  
Gene Encoding

ABSTRACT Here, we report the identification of the gene encoding a novel enzyme, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, in Burkholderia sp. HME13. The enzyme converts 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid and H2O to 3-(2,5-dioxoimidazolidin-4-yl) propionic acid and H2S. Amino acid sequence analysis of the enzyme indicates that it belongs to the DUF917 protein family, which consists of proteins of unknown function.

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