The size, shape and aggregation of tropomyosin particles

Tsao, T.-C.; Bailey, Kenneth; Adair, G. S.

doi:10.1042/bj0490027

Cited by 123 publications

(42 citation statements)

References 15 publications

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“…Below ionic strength 0·6, tropomyosin polymerizes by an end-to-end association (Tsao et al 1951). The molecular weights of the fragments were the same at ionic strength 0·06 as found in 1 M NaCl, indicating that the polymerizing properties of the parent tropomyosin were lost by cleavage at the cysteine residue.…”

Section: Characterization Of the Fragmentsmentioning

confidence: 72%

Stability of Segments of Rabbit a-Tropomyosin

Woods¹

1977

Aust. Jnl. Of Bio. Sci.

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Rabbit IX-tropomyosin was cleaved into two pieces at the cysteine residue of each chain. The products were separated by chromatography and characterized by amino acid analysis, molecular weight determination in benign and denaturing solvents, optical rotation and circular dichroism. When the cleavage reaction was carried out under mild conditions which preserve the two-chain structure there was considerable loss of IX-helix in each segment.Thermal stability studies, monitored by optical rotation and circular dichroism, showed that the transition temperature of the N-terminal fragment at pH 7·6 was approximately 17°C higher than that of the C-terminal fragment. In acid solutions there is little difference in the thermal stability of the two segments. The least stable part of the molecule is conchided to be between residues 133 and 205 and this includes the troponin-binding site. The relative stabilities found for segments of rabbit IX-tropomyosin differ from recent published conclusions and this may be a result of the different methods used to study the loss of the IX-helical conformation.The two tropomyosin fragments, unlike the parent tropomyosin, do not inhibit actomyosin adenosinetriphosphatase when mixed with troponin. The fragments did not show any of the aggregation properties of tropomyosin and did not combine with actin. The N-terminal fragment did not complex with troponin but there was some evidence for an interaction between the C-terminal fragment and troponin.

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Section: Characterization Of the Fragmentsmentioning

confidence: 72%

Stability of Segments of Rabbit a-Tropomyosin

Woods¹

1977

Aust. Jnl. Of Bio. Sci.

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“…Thermal denaturation curves ( fig.2) from the ellipticity at 2 10 nm and 222 nm gave values greater than 95% [23] An important property of the muscle tropomyosins is their ability to aggregate head-to-tail at low ionic strength, a phenomenon which results in a large increase in viscosity [24,25] . As indicated in fig.3, the relative viscosity of rabbit skeletal (Y tropomyosin increases sharply as the ionic strength is lowered below 0.1.…”

Section: Resultsmentioning

confidence: 99%

Non‐polymerizability of platelet tropomyosin and its NH₂‐ and COOH‐terminal sequences

1978

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“…The C-terminal peptide (Tm 268-284 269W) was built from residues 268-284 of the NMR structure with changes at two residues: A269W and K279N. The Nterminal peptide (ASTm [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15] ) was built from the coordinates of residues 1-15 to which an Ala-Ser N-terminal fusion dipeptide was added-residues A(21) and S(0). In this way, both peptide sequences are similar to the ones used in our binding experiments; the only difference being that tryptophan instead of 5-hydroxytryptophan was modeled at position 269.…”

Section: Protein-protein Dockingmentioning

confidence: 99%

“…9 Furthermore, Tm polymerization in vitro is strongly dependent on ionic strength. [10][11][12][13] In the first molecular model, proposed for the head-to-tail interaction by McLachlan and Stewart, 3 the complex was formed by an external overlap of the flat broad faces of the supercoil at the N-and C-termini. This model proposed the existence of intermolecular electrostatic interactions between positively charged N-terminal residues and negatively charged C-terminal residues.…”

Section: Introductionmentioning

confidence: 99%

“…Recently, a solution NMR structure of the head-to-tail complex (Tm1a [1][2][3][4][5][6][7][8][9][10][11][12][13][14] ZipTm9a 251-284 ) was solved. 14 Surprisingly, the structure showed a symmetric interleaved packing interaction in which the helical chains of the C-terminal region spread apart to allow the insertion of the N-terminal coiled-coil into the resulting cleft.…”

Section: Introductionmentioning

confidence: 99%

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Deciphering the role of the electrostatic interactions in the α‐tropomyosin head‐to‐tail complex

et al. 2008

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Skeletal α‐tropomyosin (Tm) is a dimeric coiled‐coil protein that forms linear assemblies under low ionic strength conditions in vitro through head‐to‐tail interactions. A previously published NMR structure of the Tm head‐to‐tail complex revealed that it is formed by the insertion of the N‐terminal coiled‐coil of one molecule into a cleft formed by the separation of the helices at the C‐terminus of a second molecule. To evaluate the contribution of charged residues to complex stability, we employed single and double‐mutant Tm fragments in which specific charged residues were changed to alanine in head‐to‐tail binding assays, and the effects of the mutations were analyzed by thermodynamic double‐mutant cycles and protein–protein docking. The results show that residues K5, K7, and D280 are essential to the stability of the complex. Though D2, K6, D275, and H276 are exposed to the solvent and do not participate in intermolecular contacts in the NMR structure, they may contribute to head‐to‐tail complex stability by modulating the stability of the helices at the Tm termini. Proteins 2008. © 2008 Wiley‐Liss, Inc.

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The size, shape and aggregation of tropomyosin particles

Cited by 123 publications

References 15 publications

Stability of Segments of Rabbit a-Tropomyosin

Stability of Segments of Rabbit a-Tropomyosin

Non‐polymerizability of platelet tropomyosin and its NH₂‐ and COOH‐terminal sequences

Deciphering the role of the electrostatic interactions in the α‐tropomyosin head‐to‐tail complex

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The size, shape and aggregation of tropomyosin particles

Cited by 123 publications

References 15 publications

Stability of Segments of Rabbit a-Tropomyosin

Stability of Segments of Rabbit a-Tropomyosin

Non‐polymerizability of platelet tropomyosin and its NH2‐ and COOH‐terminal sequences

Deciphering the role of the electrostatic interactions in the α‐tropomyosin head‐to‐tail complex

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Product

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Non‐polymerizability of platelet tropomyosin and its NH₂‐ and COOH‐terminal sequences