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.

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.

scholarly journals Amino acid sequences of α-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment

1978 ◽  
Vol 173 (2) ◽  
pp. 365-371 ◽  
Author(s):  
W G Crewther ◽  
A S Inglis ◽  
N M McKern
Keyword(s):  
Amino Acid ◽  
Coiled Coil ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Helical Axis ◽  
Type I ◽  
Type Ii ◽  
Coil Structure ◽  
Aqueous Urea ◽  
Alpha Keratin

1. The helical fragments obtained by partial chymotryptic digestion of S-carboxymethylkeratine-A, the low-sulphur fraction from wool, were fractionated into type-I and type-II helical segments in aqueous urea under conditions limiting carbamoylation. 2. The amino acid sequence of a 109-residue type-II segment was completed by using the sequenator. 3. When the data were incorporated into a helical model of 3.6 residues per turn the hydrophobic residues generated a band aligned at a slight angle to the helical axis. This result is in accord with the postulated coiled-coil structure of the crystalline regions of alpha-keratin.

scholarly journals Amino acid sequences of α-helical segments from S-carboxymethylkerateine-A. Statistical analysis

1978 ◽  
Vol 173 (2) ◽  
pp. 387-391 ◽  
Author(s):  
T C Elleman ◽  
W G Crewther ◽  
J Van Der Touw
Keyword(s):  
Statistical Analysis ◽  
Amino Acid ◽  
Gene Duplication ◽  
Amino Acid Residue ◽  
Coiled Coil ◽  
Amino Acid Sequences ◽  
Coil Structure ◽  
Different Types ◽  
Wool Keratin

The distribution of the different types of amino acid residue within two helical segments isolated from the low-sulphur fraction of wool keratin was examined for periodicity and larger sequence repeats. Both were detected, the former corresponding to the geometry of the proposed coiled=coil structure and the latter suggesting a distant gene duplication, though the existence of the repeat might equally well be related to interactions within the microfibril.

scholarly journals Structural studies on lamin. Similarities and differences between lamin and intermediate-filament proteins

1986 ◽  
Vol 238 (1) ◽  
pp. 305-308 ◽  
Author(s):  
D A D Parry ◽  
J F Conway ◽  
P M Steinert
Keyword(s):  
Amino Acid ◽  
Coiled Coil ◽  
Amino Acid Sequences ◽  
Ionic Interactions ◽  
Structural Studies ◽  
Intermediate Filament Proteins ◽  
Coiled Coil Domain ◽  
Similarities And Differences ◽  
Almost Continuous

Analysis of the amino acid sequences of lamins A and C has revealed that each chain has an almost continuous heptad-containing coiled-coil domain containing structural regularities in the linear disposition of the acidic and the basic residues. The data suggest that the lamin molecules are two-stranded ropes, that the two chains are parallel to one another and in axial register, and that the molecules aggregate in vivo through periodic ionic interactions. These results indicate that significant changes in stability of the nuclear envelope may be achieved between interphase and mitosis through changes in the degree of phosphorylation of the lamin proteins.

scholarly journals The amino acid sequence of cysteic acid-containing peptides from performic acid-oxidized ovotransferrin

1970 ◽  
Vol 116 (3) ◽  
pp. 515-532 ◽  
Author(s):  
T. C. Elleman ◽  
J. Williams
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Sequences ◽  
Performic Acid ◽  
Cysteic Acid ◽  
Cystine Content

1. The half-cystine content of ovotransferrin, measured as cysteic acid, was 31mol/80000g of protein. 2. The amino acid sequences of cysteic acid-containing peptides from performic acid-oxidized ovotransferrin were studied. 3. 34 unique cysteic acid residues were identified. 4. It is concluded that hen ovotransferrin does not consist of two identical halves or subunits.

scholarly journals Disulphide bridges of the heavy chain of human immunoglobulin G2

1971 ◽  
Vol 121 (2) ◽  
pp. 217-225 ◽  
Author(s):  
C. Milstein ◽  
B. Frangione
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Amino Acid Sequences ◽  
Cysteic Acid ◽  
Partial Reduction ◽  
Variable Part ◽  
One Dimensional ◽  
Heavy Chains ◽  
Dimensional Electrophoresis

Amino acid sequences around the disulphide bridges of the heavy chain of an immunoglobulin of the γ2 subclass have been studied. The protein was digested with pepsin and the digest fractionated by Sephadex. Screening of the eluate by one-dimensional electrophoresis of oxidized and unoxidized samples was used as an assay and pools of fractions were prepared. Identification by diagonal electrophoresis of several inter- and intra-chain disulphide bridges was done on the pooled fractions. The inter-heavy-chain bridged peptide included four cystine residues. Comparison with proteins of other human subclasses indicated that the intrachain bridges identified are the bridges of the invariable section of γ2 heavy chains. The amino acid sequence of one cysteic acid peptide that may have been derived from the variable part of the molecule was determined. Partial reduction followed by carboxymethylation with radioactive iodoacetate of two proteins of the γ2 class showed a number of labelled peptides that could be identified as being related to the inter-chain bonded cystine residues.

scholarly journals Amino acid sequences of α-helical segments from S-carbosymethylkerateine-A. Complete sequence of a type-I segment

1978 ◽  
Vol 173 (2) ◽  
pp. 373-385 ◽  
Author(s):  
K H Gough ◽  
A S Inglis ◽  
W G Crewther
Keyword(s):  
Amino Acid ◽  
Sequence Data ◽  
Coiled Coil ◽  
Alpha Helix ◽  
Protein S ◽  
Amino Acid Sequences ◽  
Type I ◽  
Type Ii ◽  
Sequencing Data ◽  
Helical Segment

The amino acid sequence of a type-I helical segment from the low-sulphur protein (S-carboxymethylkerateine-A) of wool was determined by combining automatic and manual-sequencing data. Whereas in the type-II helical segment most of the cationic groups occur in pairs, 11 of the 22 anionic residues in the sequence of the type-I segment were situated next to a second anionic residue. This suggests possible interactions between type-I and type-II helical segments in alpha-keratin. As observed with the sequence of a type-II helical segment a model constructed on 3.6 residues per turn of helix shows a line of hydrophobic residues along the helix, thereby supporting the physicochemical evidence that the molecule is predominantly helical and forms part of a coiled-coil structure. Examination of the sequence data by predictive methods indicates the possibilty of extensive sections of alpha-helix interspersed with discontinuities. The molecule contains a number of regions with peptide sequences identical with those found by other workers after enzymic digestion of fractions from oxidized wool.

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