Literature DB >> 9017208

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

E A Czuryło1, T Hellweg, W Eimer, R Dabrowska.   

Abstract

The size and the shape of caldesmon as well as its 50-kDa central and 19-kDa C-terminal fragments were investigated by photon correlation spectroscopy. The hydrodynamic radii, which have been calculated from the experimentally obtained translational diffusion coefficients, are 9.8 nm, 6.0 nm, and 2.9 nm, respectively. Moreover, the experimental values for the translational diffusion coefficients are compared with results obtained from hydrodynamic model calculations. Detailed models for the structure of caldesmon in solution are derived. The contour length is about 64 nm for all of the models used for caldesmon.

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Year:  1997        PMID: 9017208      PMCID: PMC1185606          DOI: 10.1016/s0006-3495(97)78717-4

Source DB:  PubMed          Journal:  Biophys J        ISSN: 0006-3495            Impact factor:   4.033


  43 in total

Review 1.  Caldesmon, a novel regulatory protein in smooth muscle and nonmuscle actomyosin systems.

Authors:  K Sobue; J R Sellers
Journal:  J Biol Chem       Date:  1991-07-05       Impact factor: 5.157

2.  Parallel inhibition of active force and relaxed fiber stiffness in skeletal muscle by caldesmon: implications for the pathway to force generation.

Authors:  B Brenner; L C Yu; J M Chalovich
Journal:  Proc Natl Acad Sci U S A       Date:  1991-07-01       Impact factor: 11.205

3.  A long helix from the central region of smooth muscle caldesmon.

Authors:  C L Wang; J M Chalovich; P Graceffa; R C Lu; K Mabuchi; W F Stafford
Journal:  J Biol Chem       Date:  1991-07-25       Impact factor: 5.157

Review 4.  The molecular anatomy of caldesmon.

Authors:  S B Marston; C S Redwood
Journal:  Biochem J       Date:  1991-10-01       Impact factor: 3.857

5.  Spectrofluorimetric studies on C-terminal 34 kDa fragment of caldesmon.

Authors:  E A Czuryło; V I Emelyanenko; E A Permyakov; R Dabrowska
Journal:  Biophys Chem       Date:  1991-05       Impact factor: 2.352

6.  Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon.

Authors:  L Velaz; R H Ingraham; J M Chalovich
Journal:  J Biol Chem       Date:  1990-02-15       Impact factor: 5.157

7.  Electron microscopic studies of chicken gizzard caldesmon and its complex with calmodulin.

Authors:  K Mabuchi; C L Wang
Journal:  J Muscle Res Cell Motil       Date:  1991-04       Impact factor: 2.698

8.  Caldesmon and the structure of smooth muscle thin filaments: electron microscopy of isolated thin filaments.

Authors:  C Moody; W Lehman; R Craig
Journal:  J Muscle Res Cell Motil       Date:  1990-04       Impact factor: 2.698

9.  Localization and characterization of a 7.3-kDa region of caldesmon which reversibly inhibits actomyosin ATPase activity.

Authors:  J M Chalovich; J Bryan; C E Benson; L Velaz
Journal:  J Biol Chem       Date:  1992-08-15       Impact factor: 5.157

Review 10.  The Ayerst Award Lecture 1990. Calcium-dependent mechanisms of regulation of smooth muscle contraction.

Authors:  M P Walsh
Journal:  Biochem Cell Biol       Date:  1991-12       Impact factor: 3.626

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  1 in total

1.  Dynamic light scattering study of calmodulin-target peptide complexes.

Authors:  Andriyka L Papish; Leslie W Tari; Hans J Vogel
Journal:  Biophys J       Date:  2002-09       Impact factor: 4.033

  1 in total

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