scholarly journals Curvature autocorrelations in domain growth dynamics

1999 ◽  
Vol 9 (4) ◽  
pp. 719-724 ◽  
Author(s):  
O.L. Schönborn ◽  
R.C. Desai
2019 ◽  
Vol 54 (15) ◽  
pp. 10600-10608 ◽  
Author(s):  
Jiayu Pan ◽  
Tianlu Men ◽  
Xingyu Xu ◽  
Ze Xu ◽  
Qi Li ◽  
...  

2010 ◽  
Vol 96 (1) ◽  
pp. 012908 ◽  
Author(s):  
Yunseok Kim ◽  
Wooyoung Kim ◽  
Hyunwoo Choi ◽  
Seungbum Hong ◽  
Hyungsoo Ko ◽  
...  

2017 ◽  
Vol 43 (12) ◽  
pp. 9538-9542 ◽  
Author(s):  
Tian-Lu Men ◽  
Hao Cheng Thong ◽  
Jun-Tao Li ◽  
Mo Li ◽  
Jian Zhang ◽  
...  

2006 ◽  
Vol 73 (5) ◽  
Author(s):  
Peter Heinig ◽  
César Márquez Beltrán ◽  
Dominique Langevin

1993 ◽  
Vol 04 (03) ◽  
pp. 701-720 ◽  
Author(s):  
EDUARD VIVES ◽  
ANTONI PLANES

Domain growth dynamics in binary alloys undergoing an order-disorder phase transition is revised. After a summary of the state-of-the-art of the problem, we focus on the Monte Carlo simulation results. The usual atom-exchange dynamics is compared with a more realistic vacancy driven dynamics. Results suggest that the expected Allen-Cahn growth law might be modified by this more realistic dynamics.


2021 ◽  
Vol 8 ◽  
Author(s):  
Nitzan Maman ◽  
Pramod Kumar ◽  
Amarjeet Yadav ◽  
Mario Feingold

In the Escherichia coli, RecA plays a central role in the recombination and repair of the DNA. For homologous recombination, RecA binds to ssDNA forming a nucleoprotein filament. The RecA-ssDNA filament searches for a homologous sequence on a dsDNA and, subsequently, RecA mediates strand exchange between the ssDNA and the dsDNA. In vitro, RecA binds to both ssDNA and dsDNA. Despite a wide range of studies of the polymerization of RecA on dsDNA, both at the single molecule level and by means of biochemical methods, important aspects of this process are still awaiting a better understanding. Specifically, a detailed, quantitative description of the nucleation and growth dynamics of the RecA-dsDNA filaments is still lacking. Here, we use Optical Tweezers together with a single molecule analysis approach to measure the dynamics of the individual RecA domains on dsDNA and the corresponding growth rates for each of their fronts. We focus on the regime where the nucleation and growth rate constants, kn and kg, are comparable, leading to a coverage of the dsDNA molecule that consists of a small number of RecA domains. For the case of essentially irreversible binding (using ATPγS instead of ATP), we find that domain growth is highly asymmetric with a ratio of about 10:1 between the fast and slow fronts growth rates.


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