The transient state in the oxidation of binary alloys forming the most-stable oxide: A numerical solution

1997 ◽  
Vol 47 (5-6) ◽  
pp. 507-524 ◽  
Author(s):  
F. Gesmundo ◽  
M. Pereira

1997 ◽  
Vol 47 (1-2) ◽  
pp. 91-115 ◽  
Author(s):  
F. Gesmundo ◽  
P. Castello ◽  
F. Viani ◽  
J. Philibert




1996 ◽  
Vol 46 (5-6) ◽  
pp. 383-398 ◽  
Author(s):  
F. Gesmundo ◽  
P. Castello ◽  
F. Viani


2020 ◽  
Vol MA2020-02 (9) ◽  
pp. 1176-1176
Author(s):  
Penghao Xiao ◽  
Brandon C. Wood




2012 ◽  
Vol 326-328 ◽  
pp. 120-125 ◽  
Author(s):  
V.S.O. Farias ◽  
Wilton Pereira Silva ◽  
C.M.D.P. Silva e Silva ◽  
Antônio Gilson Barbosa de Lima

This work presents a three-dimensional numerical solution for the diffusion equation in transient state, in an arbitrary domain. For this end, the diffusion equation was discretized using the finite volume method with a fully implicit formulation and generalized coordinates, for the equilibrium boundary condition. For each time step, the system of equations obtained for a given structured mesh was solved by the Gauss-Seidel method. The computational code was developed in FORTRAN, using the CFV 6.6.0 Studio, in a Windows platform. The proposed solution was validated using analytical and numerical solutions of the diffusion equation for different geometries (orthogonal and non-orthogonal meshes). The analysis and comparison of the results showed that the proposed solution provides correct results for the cases investigated. The developed computational code was applied in the simulation of the drying of ceramic roof tiles for the following temperature: 55.6 °C. The analysis of the results makes it possible to affirm that the developed numerical solution satisfactorily describes the drying processes in this temperature.



1997 ◽  
Vol 47 (3-4) ◽  
pp. 215-235 ◽  
Author(s):  
F. Gesmundo ◽  
P. Castello ◽  
F. Viani


1997 ◽  
Vol 47 (3-4) ◽  
pp. 355-380 ◽  
Author(s):  
F. Gesmundo ◽  
F. Viani ◽  
Y. Niu


Author(s):  
Jeff Gelles

Mechanoenzymes are enzymes which use a chemical reaction to power directed movement along biological polymer. Such enzymes include the cytoskeletal motors (e.g., myosins, dyneins, and kinesins) as well as nucleic acid polymerases and helicases. A single catalytic turnover of a mechanoenzyme moves the enzyme molecule along the polymer a distance on the order of 10−9 m We have developed light microscope and digital image processing methods to detect and measure nanometer-scale motions driven by single mechanoenzyme molecules. These techniques enable one to monitor the occurrence of single reaction steps and to measure the lifetimes of reaction intermediates in individual enzyme molecules. This information can be used to elucidate reaction mechanisms and determine microscopic rate constants. Such an approach circumvents difficulties encountered in the use of traditional transient-state kinetics techniques to examine mechanoenzyme reaction mechanisms.



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