𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Diffusion of vacancy-impirity-paris in cystalline solids studied by a Monte Carlo simulation

✍ Scribed by Dr. B. Fritzsch; Prof. Dr. Dr. h. c. A. Zehe

Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
306 KB
Volume
29
Category
Article
ISSN
0232-1300

No coin nor oath required. For personal study only.

✦ Synopsis

The joint migration of vacancy-impurity-pairs (VIPs) in dilute metallic alloys has been used in a previous publication to explain void formation resistance in electromigration experiments for certain material combinations. A corresponding rule is based on the valency of matrix and alloying elements. This paper deals with the range of validity of that rule, considering thermodynamic parameters like binding and migration energy as well as temperature, which are incorporated in a Monte Carlo simulation of the migration process of VIPs. Rule exceptions are explained by the outcome of this analysis. c u Ag 0 no D 0.54[3] ... 0.82[4] no Ag c u 0 no D 1.04[3] no Al c u 2 no D 0.89[5] ___ 1.1316) no c u In 2 no D no Ag* Zn 1 yes D 0.96[3] no Cu* Zn

📜 SIMILAR VOLUMES

The importance of axonal undulation in d
The importance of axonal undulation in diffusion MR measurements: a Monte Carlo simulation study
✍ Markus Nilsson; Jimmy Lätt; Freddy Ståhlberg; Danielle van Westen; Håkan Hagslät 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 348 KB

Many axons follow wave‐like undulating courses. This is a general feature of extracranial nerve segments, but is also found in some intracranial nervous tissue. The importance of axonal undulation has previously been considered, for example, in the context of biomechanics, where it has been shown th

A pH-dependent variation in α-helix stru
A pH-dependent variation in α-helix structure of the S-peptide of ribonuclease A studied by Monte Carlo simulated annealing
✍ Takashi Nakazawa; Sumiko Ban; Yuka Okuda; Masato Masuya; Ayori Mitsutake; Yuko O 📂 Article 📅 2002 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 386 KB 👁 1 views

## Abstract Low‐energy conformations of the S‐peptide fragment (20 amino acid residues long) of ribonuclease A were studied by Monte Carlo simulated annealing. The obtained lowest‐energy structures have α‐helices with different size and location, depending distinctively on the ionizing states of ac