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B Roux

Publications and source records attributed to B Roux.

120 records · Page 7Linked to original sources
PubMed1982

Differences in the electric birefringence of spectrin dimers and tetramers as shown by the fast reversing electric pulse method.

The electric birefringence of purified spectrin has been examined in medium of low ionic strength at 20 degrees C and for electric fields smaller than 4 X 10(4) V m(-1), using the reversing electric pulse method. This technique allows study of the permanent and induced dipole electric moment of macromolecules more easily than in measurements using only rectangular pulses. We show that spectrin heterodimers and heterotetramers have different electro-optical properties. The relaxation time of the tetramer (7 microseconds) is significantly longer than that of the dimer (4.5 microseconds). Tetramers and dimers have also different polarizability parameters.

Birefringence↗
PubMed1981

Conformation of chromatin oligomers. A new argument for a change with the hexanucleosome.

Quasielastic laser light scattering measurements have been made on chromatin oligomers to obtain information on the transition in their electrooptical properties, previously observed for the hexameric structures [Marion, C. and Roux, B. (1978) Nucleic Acids Res. 5, 4431-4449]. Translational diffusion coefficients were determined for mononucleosomes to octanucleosomes containing histone H1 over a range of ionic strength. At high ionic strength, oligomers show a linear dependence of the logarithm of diffusion coefficient upon the logarithm of number of nucleosomes. At low ionic strength a change occurs between hexamer and heptamer. Our results agree well with the recent sedimentation data of Osipova et al. [Eur. J. Biochem. (1980) 113, 183-188] and of Butler and Thomas [J. Mol. Biol. (1980) 140, 505-529] showing a change in stability with hexamer. Various models for the arrangements of nucleosomes in the superstructure of chromatin are discussed. All calculations clearly indicate a conformational change with the hexanucleosome and the results suggest that, at low ionic strength, the chromatin adopts a loosely helical structure of 28-nm diameter and 22-nm pitch. These results are also consistent with a discontinuity every sixth nucleosome, corresponding to a turn of the helix. This discontinuity may explain the recent electric dichroism data of Lee et al. [Biochemistry (1981) 20, 1438-1445]. The hexanucleosome structure which we have previously suggested, with the faces of nucleosomes arranged radially to the helical axis has been recently confirmed by Mc Ghee et al. [Cell (1980) 22, 87-96]. With an increase of ionic strength, the helix becomes more regular and compact with a slightly reduced outer diameter and a decreased pitch, the dimensions resembling those proposed for solenoid models.

Animals↗
PubMed1978

Intermolecular interaction studies on native and enzyme-treated acid-soluble collagen.

The aggregative properties of acid-soluble collagen, native or enzyme treated, have been studied by electric birefringence and low shear rate viscosity. A unique type of aggregate has been found, about 700 nm long for native collagen and 530 nm for pepsin treated, regardless of the acetic acid concentration in the range 1--100 mM. The number of aggregates increases with collagen concentrations, as could be expected for electrostatic interactions. On the contrary, pepsin-extracted cartilage collagen forms aggregates of covalent nature, the number of which is independent of concentration. Viscosity measurements show two different interaction mechanisms: a short distance one which can be identified with the electric birefringence-detected aggregation, and a long distance superstructure which disappears when salt is added to the solution.

Acetates↗
PubMed1978

Nucleosomes arrangement in chromatin.

The spatial arrangement of nucleosomes in rat liver chromatin has been examined using the electric birefringence technique. All chromatin subunits studied (up to 9 consecutive nucleosomes) contain their full complement of the five histone types associated with about 200 base pairs repeat length DNA. From the relaxation times and the orientation mechanisms, the nucleosome may be assimilated to an oblate ellipsoid of dimensions about 140 x 140 x 70 A, and the DNA superhelical axis is parallel to its shorter axis. The most important result is a sharp transition in the electro-optical properties of subunits when the number of nucleosomes in the chain is greater than 6 : the initial negative birefringence, as for DNA, becomes positive and the relaxation time is multiplied by ten. The hexanucleosome, which presents no birefringence, has an helical symmetrical structure without preferential orientation axis. This structure is approximatively spherical of about 250 A diameter and the chromatin appears as a periodic array of such a structure.

Animals↗
PubMedDate not supplied

An algorithm for protein secondary structure prediction based on class prediction.

An algorithm has been developed to improve the success rate in the prediction of the secondary structure of proteins by taking into account the predicted class of the proteins. This method has been called the 'double prediction method' and consists of a first prediction of the secondary structure from a new algorithm which uses parameters of the type described by Chou and Fasman, and the prediction of the class of the proteins from their amino acid composition. These two independent predictions allow one to optimize the parameters calculated over the secondary structure database to provide the final prediction of secondary structure. This method has been tested on 59 proteins in the database (i.e. 10,322 residues) and yields 72% success in class prediction, 61.3% of residues correctly predicted for three states (helix, sheet and coil) and a good agreement between observed and predicted contents in secondary structure.

Algorithms↗