Literature DB >> 8343116

Studies on secondary structure of caldesmon and its C-terminal fragments.

E A Czuryło1, R Dabrowska.   

Abstract

Evaluation of the secondary structure of caldesmon from c.d. spectra revealed that it contains 51% helix, 9% beta-strand and 40% of remainder structures. These values agree well with the predicted ones from amino acid sequence, assuming an extended chain structure for caldesmon. The estimates of the secondary-structure elements in C-terminal 34 kDa and 19 kDa fragments are: 11 and 12% helix, 22 and 20% beta-strand, 13 and 17% beta-turns and loops, and 54 and 50% of remainder structure respectively. The best fit of experimental data was obtained assuming the globular state of the fragments. On the basis of structural analysis and fragmentation by proteolytic and chemical cleavages the six-domain model of caldesmon is proposed.

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Year:  1993        PMID: 8343116      PMCID: PMC1134368          DOI: 10.1042/bj2930363

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  26 in total

1.  Inhibition of actin-tropomyosin activation of myosin MgATPase activity by the smooth muscle regulatory protein caldesmon.

Authors:  S B Marston; C S Redwood
Journal:  J Biol Chem       Date:  1992-08-25       Impact factor: 5.157

2.  Further developments of protein secondary structure prediction using information theory. New parameters and consideration of residue pairs.

Authors:  J F Gibrat; J Garnier; B Robson
Journal:  J Mol Biol       Date:  1987-12-05       Impact factor: 5.469

3.  Functional domain of caldesmon.

Authors:  A Szpacenko; R Dabrowska
Journal:  FEBS Lett       Date:  1986-07-07       Impact factor: 4.124

4.  Calculation of protein conformation from circular dichroism.

Authors:  J T Yang; C S Wu; H M Martinez
Journal:  Methods Enzymol       Date:  1986       Impact factor: 1.600

5.  Correction of light-scattering errors in spectrophotometric protein determinations.

Authors:  A F Winder; W L Gent
Journal:  Biopolymers       Date:  1971       Impact factor: 2.505

6.  Estimation of globular protein secondary structure from circular dichroism.

Authors:  S W Provencher; J Glöckner
Journal:  Biochemistry       Date:  1981-01-06       Impact factor: 3.162

7.  Theory of protein secondary structure and algorithm of its prediction.

Authors:  O B Ptitsyn; A V Finkelstein
Journal:  Biopolymers       Date:  1983-01       Impact factor: 2.505

8.  Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties.

Authors:  A Bretscher
Journal:  J Biol Chem       Date:  1984-10-25       Impact factor: 5.157

9.  Smooth muscle caldesmon is an extended flexible monomeric protein in solution that can readily undergo reversible intra- and intermolecular sulfhydryl cross-linking. A mechanism for caldesmon's F-actin bundling activity.

Authors:  W P Lynch; V M Riseman; A Bretscher
Journal:  J Biol Chem       Date:  1987-05-25       Impact factor: 5.157

10.  Optical characteristics of all individual proteins from the small subunit of Escherichia coli ribosomes.

Authors:  S Y Venyaminov; Z V Gogia
Journal:  Eur J Biochem       Date:  1982-08
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  2 in total

1.  Modulation of gelsolin-induced actin-filament severing by caldesmon and tropomyosin and the effect of these proteins on the actin activation of myosin Mg(2+)-ATPase activity.

Authors:  R Dabrowska; H Hinssen; B Gałazkiewicz; E Nowak
Journal:  Biochem J       Date:  1996-05-01       Impact factor: 3.857

2.  The size and shape of caldesmon and its fragments in solution studied by dynamic light scattering and hydrodynamic model calculations.

Authors:  E A Czuryło; T Hellweg; W Eimer; R Dabrowska
Journal:  Biophys J       Date:  1997-02       Impact factor: 4.033

  2 in total

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