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J Gomel

Publications and source records attributed to J Gomel.

3 recordsLinked to original sources

A fast algorithm for evaluating an approximation to the information enclosed within coronas and their sectors in square matrices.

From numerical data distributed in an even square matrix A, we wish to determine the proportion of the data belonging to a selected area (S). We restrict the problem to any field of the initial data square enclosed within the part of a corona (characterized by the real values of its two limiting radii) limited by a circular sector (defined by its two limiting angles), both corona and sector being centred at the centre of the square. A fast and accurate approximation algorithm is presented, which collects the contribution of all the pixels of A by exploration of the first quadrant. For each pixel of it and, at the same time, for its three symmetrical ones in the other quadrants, the program evaluates the part belonging to (S), using radial and angular factors. Finally, the weighted contributions are summed up. Compared to the classical methods (exact determination, testing the position of the pixel centres or others), this algorithm offers a better time/accuracy ratio. Suitable accuracy at the border makes it possible to choose larger pixel size, hence to spend shorter CPU time (even and especially in the case of thin rings with large radii).

Algorithms↗

Image analysis of the heavy form of the acetylcholine receptor from Torpedo marmorata.

The structure of the heavy (H) form of the acetylcholine receptor, which comprises two covalently linked 250,000 Mr oligomers, has been investigated by numerical analysis of electron microscope images. Na-cholate solubilized Torpedo marmorata H-form receptor was reintegrated into artificial lipid vesicles and negatively stained with uranyl acetate prior to imaging in a conventional transmission microscope. The reconstituted preparations exhibited the standard polypeptide composition of the purified receptor (alpha 2 beta gamma delta) and the same transmembrane arrangement as in the native subsynaptic membrane. Covalent disulfide linkage between the two oligomers took place exclusively through the delta chains. In agreement with previous work (Cartaud et al., 1980) the H-form appeared as "doublets" of two coplanar 9 nm rosettes at a center-to-center distance of 9.2 +/- 1.1 nm. The relative angular orientation of the two rosettes in a doublet was examined by correlation analysis in the real space. It exhibited a marked variability, few of the doublets featuring any kind of symmetry, suggesting that the two oligomers of a doublets are connected via an extended and flexible chain or loop. The area of contact between the two rosettes of a doublet therefore does not necessarily represent a reliable clue as to the location of the delta chain within the structure. Averaged images obtained after reorientation and summation of up to 132 rosettes revealed the three major peaks and the two grooves already observed in previous studies. Two additional smaller peaks were identified. Tentative assignment of structural details to individual subunits was deduced from an examination of alpha-bungarotoxin-labeled doublets. The alpha subunits, which carry part or all of the acetylcholine binding sites, are probably located in nonadjacent positions in the vicinity of the newly found peaks. This assignment is consistent with the image analysis of receptor-toxin complexes recently reported by Zingsheim et al. (1982b).

Animals↗

[Relative orientation of the two oligomers composing the heavy form of the acetylcholine receptor from Torpedo marmorata].

The morphology of the heavy form (H) of the nicotinic acetylcholine receptor reintegrated into lipid vesicles after purification in the presence of sodium cholate is studied by numerical analysis of electron microscopy images obtained after negative staining. The analysis discloses a large variability in the relative orientation of the two alpha 2 beta gamma delta oligomers (L), suggesting a flexible mode of association between oligomers through the delta chains.

Animals↗