Laser Beam Lithography for Direct Patterning of Interconnections on Prediffused ASIC's

Fleury, A.; Saint-Christophe, Emmanuel; Frémont, Hélène; Fathi, Mohammed; N’Kaoua, Gilles; Danto, Yves

doi:10.1051/jp3:1995203

J. Phys. III France

1995

DOI: 10.1051/jp3:1995203

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Laser Beam Lithography for Direct Patterning of Interconnections on Prediffused ASIC's

A. Fleury¹,

Emmanuel Saint-Christophe²,

Hélène Frémont³

et al.

Abstract: A lithography machine designed for laser direct writing of metallisation in ASIC'S and MCM, and the associated practical process are described.To demonstrate the feasibility of the laser direct writing, the last level of metallisation on a bipolar ASIC has been drawn. The design rules have been calculated using a theoretical modelling of the interaction between laser beam and photoresists.Calculation and experiment are in good agreement for two kinds of photoresists.1.

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2001

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Competition between protein folding and aggregation: A three-dimensional lattice-model simulation

Bratko

Blanch

2001

The Journal of Chemical Physics

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Aggregation of protein molecules resulting in the loss of biological activity and the formation of insoluble deposits represents a serious problem for the biotechnology and pharmaceutical industries and in medicine. Considerable experimental and theoretical efforts are being made in order to improve our understanding of, and ability to control, the process. In the present work, we describe a Monte Carlo study of a multichain system of coarse-grained model proteins akin to lattice models developed for simulations of protein folding. The model is designed to examine the competition between intramolecular interactions leading to the native protein structure, and intermolecular association, resulting in the formation of aggregates of misfolded chains. Interactions between the segments are described by a variation of the Go potential [N. Go and H. Abe, Biopolymers 20, 1013 (1981)] that extends the recognition between attracting types of segments to pairs on distinct chains. For the particular model we adopt, the global free energy minimum of a pair of protein molecules corresponds to a dimer of native proteins. When three or more molecules interact, clusters of misfolded chains can be more stable than aggregates of native folds. A considerable fraction of native structure, however, is preserved in these cases. Rates of conformational changes rapidly decrease with the size of the protein cluster. Within the timescale accessible to computer simulations, the folding-aggregation balance is strongly affected by kinetic considerations. Both the native form and aggregates can persist in metastable states, even if conditions such as temperature or concentration favor a transition to an alternative form. Refolding yield can be affected by the presence of an additional polymer species mimicking the function of a molecular chaperone.

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Competition between protein folding and aggregation: A three-dimensional lattice-model simulation

Bratko

Blanch

2001

The Journal of Chemical Physics

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show abstract

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Laser Beam Lithography for Direct Patterning of Interconnections on Prediffused ASIC's

Cited by 1 publication

References 3 publications

Competition between protein folding and aggregation: A three-dimensional lattice-model simulation

Competition between protein folding and aggregation: A three-dimensional lattice-model simulation

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