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Tropomyosin amino acid sequences

Hodges, R. S., Sodek, J., Smillie, L. B., and Jurasek, L. (1972). Tropomyosin Amino acid sequence and coiled-coil structure. Cold Spring Harh. Symp. Quant. Biol. 37, 299-310. [Pg.153]

While invertebrate tropomyosins are likely pan-allergens, vertebrate tropomyosins appear to be nonallergenic (Reese et ah, 1999). Using bioinformatics approaches to compare the sequences of tropomyosins from various species, Goodman et ah (2002) determined that tropomyosins from vertebrate species — rabbit, pig, chicken, and human — share 53-57% amino acid sequence identity to the known shrimp tropomyosin allergen. Met e 1. This comparison likely explains why vertebrate tropomyosins are not allergenic and do not cross-react with IgE antibodies specific to invertebrate tropomyosins. [Pg.161]

Stone, D., and Smillie, L. B. (1978). The amino acid sequence of rabbit skeletal a-tropomyosin The N-terminal half and complete sequence. J. Biol. Chem. 253, 1137-1148. [Pg.88]

Parry, D. A. (1981). Analysis of the amino acid sequence of a tropomyosin-binding fragment from troponin-T. / Mol. Biol. 146, 259-263. [Pg.156]

This interaction pattern is also reflected in the amino acid sequences of proteins such as tropomyosin, which can be shown to be composed of a basic seven-residue sequence that is repeated 40 times without interruption (Hodges et al., 1972 McLachlan and Stewart, 1975). Hydrophobic residues almost invariably occupy the second and fifth positions of the heptad and are presumably directed toward the major axis of the superhelix, where they serve to stabilize the structure by hydrophobic effects (Fig. 15). The charged side chains are also nonrandomly distributed and are believed to form interhelical ion pairs that further stabilize the structure (Talbot and Hodges, 1982). [Pg.103]

Furthermore, it was shown that there are three different isoforms of tropomyosin relating to different functional needs (fast, slow-twitch, and slow-tonic), identified by amino acid sequence analysis (Motoyama et al. 2007). The fast isoform is mostly found in the abdominal muscle (tail), while the slow isoform is mainly associated with muscle obtained from the legs however, both forms can be found in abdominal and leg muscle, with an amino acid homology of up to 100%. [Pg.239]

Even though IgE cross-reactivity among crustaceans and mollusks are commonly reported until recently, limited work has been done on the molecular identity of these cross-reactive allergens. The amino acid sequence identity with shrimp tropomyosin is fairly low with 57% and 61% for mussels and abalone, respectively (Figure 9.1). The relationship of molecular cross-reactivity with clinical reactivity has however not been adequately defined. [Pg.248]

The discussion above stresses the importance of the CN4 region (residues 96-116) of troponin I in the inhibition of contractile interaction of myosin-actin in the presence of tropomyosin. The amino acid sequence of the CN4 region is shown in Fig. 3. Talbot and Hodges (1981) synthesized 12 peptide analogs of the CN4 sequence and examined their inhibitory action on actomyosin ATPase activity. The absence of residues 115 and 116 did not affect the activity, whereas the absence of residue 114 significantly decreased the inhibitory action. As to the N-terminal portion of the peptide, residues 96-103 were not essential, but the absence of Lys-105 decreased the inhibitory activity. A peptide containing the region of residues Lys-105-Val-l 14 showed about half of the inhibitory action of troponin I. The authors concluded that Lys-105 and the bulky side chain at Val-114 are essential for the inhibitory action of troponin I (Fig. 3). [Pg.11]

The amino acid sequence of a and /3 subunits of tropomyosin from rabbit skeletal muscle has been determined (Stone and Smillie, 1978 Sodek et al, 1978 Mak et al, 1980). Both subunits consist of a single peptide of 284 amino acid residues. The N-terminal residue is acetylated methionine, and the C-terminal residues is He. Assuming that all resi-... [Pg.31]

The amino acid sequence of the /8-tropomyosin subunit is mostly the same as that of a-tropomyosin, with the difference being 39 residues. Most residues were replaced by the same family of amino acid residues, with the exception that Ser-229 and His-276 in the a-subunit are replaced by Glu-229 and Asn-276 in the /8-subunit. Hence, /3-tropomyosin is a little more acidic than a-tropomyosin (Mak et ai, 1980). [Pg.33]

The structure mentioned above is by no means a unique solution for the structure of tropomyosin and troponin. But it is certain that these studies are useful in integrating the enormous amount of experimental evidence, and in visualizing how Ca " changes the troponin complex at the level of the amino acid sequence. Information on the interacting regions of the actin molecule for tropomyosin and troponin I will surely lead to another breakthrough for this line of approaches. [Pg.50]

Tropomyosin is a muscle protein, and has an unusual amino acid sequence consisting of seven residues, (a-b-c-d-e-f-g) . There is the tendency for hydro-phobic amino acid residues to be located at positions a and d in this sequence, and in many cases, the hydrophilic amino acid residues are in other positions (b, c, e, f and g). It has been suggested that this sequence forms coiled-coil a-helix ropes, which is one of the supersecondary structures of proteins. A schematic picture of the cross-section of the coiled-coil structure is shown in Fig. 23.21. [Pg.882]

By examining the amino add sequence of tropomyosin, the smallest and simplest proteins postulated at the time 1819 to contain the coiled-coil motif, we identified the hydrophobic repeat responsible for the formation and stabilization of the coiled-coil structure. 18 A coiled coil can be considered as a repeating heptad of seven amino acid residues a-b-c-d-e-f-g, where positions a and d are occupied by hydrophobic residues. This 3-4 (or 4-3) hydro-... [Pg.68]

C -Keratin, which is the primary component of wool and hair, consists of two right-handed o helices intertwined to form a type of left-handed superhelix called an a coiled coil, ot-Keratin is a member of a superfamily of proteins referred to as coiled-coil proteins (Figure 2,43). In these proteins, two or more a helices can entwine to form a verv stable structure, which can have a length of 1000 A (100 nm, or 0.1 jiim) or more. There are approximately 60 members of this family in humans, including intermediate filaments, proteins that contribute to the cell cytoskeleton (internal scaffolding in a cell), and the muscle proteins myosin and tropomyosin (Section 34.2). Members of this family are characterized by a central region of 300 amino acids that contains imperfect repeats ol a sequence of seven amino acids called a heptad repeal. [Pg.44]


See other pages where Tropomyosin amino acid sequences is mentioned: [Pg.160]    [Pg.161]    [Pg.164]    [Pg.164]    [Pg.166]    [Pg.166]    [Pg.1647]    [Pg.3]    [Pg.144]    [Pg.156]    [Pg.239]    [Pg.242]    [Pg.10]    [Pg.24]    [Pg.25]    [Pg.29]    [Pg.49]    [Pg.876]    [Pg.232]    [Pg.63]    [Pg.85]    [Pg.734]    [Pg.713]    [Pg.379]    [Pg.362]    [Pg.723]    [Pg.351]    [Pg.142]    [Pg.92]    [Pg.243]    [Pg.246]    [Pg.249]    [Pg.33]   
See also in sourсe #XX -- [ Pg.123 ]

See also in sourсe #XX -- [ Pg.66 , Pg.67 , Pg.68 , Pg.69 ]




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