Logical gates in actin monomer.
1University of the West of England, Bristol, BS16 1QY, United Kingdom. andrew.adamatzky@uwe.ac.uk.
Scientific Reports
|September 20, 2017
Summary
Single actin molecules can process information by implementing logical gates through excitation patterns. This research explores their potential as molecular computers, demonstrating basic computational circuits.
Area of Science:
- Biophysics
- Molecular Computing
- Computational Biology
Background:
- Actin molecules play crucial roles in cellular processes.
- Understanding molecular information processing is key to developing novel computing paradigms.
- Excitable media can exhibit complex computational behaviors.
Purpose of the Study:
- To evaluate the information processing capacity of a single actin molecule.
- To determine the types of logical gates implemented by actin molecules.
- To explore the potential of actin-based systems for molecular computation.
Main Methods:
- Representing filamentous actin as an excitable automaton network (F-actin automaton).
- Modeling atom state updates based on chemical bonds (hard neighbors) and physical proximity (soft neighbors).
- Analyzing propagating patterns of excitation to identify implemented logical gates.
Main Results:
- F-actin automata were shown to implement OR, AND, XOR, and AND-NOT logical gates.
- The AND gate was found to be the most common, while XOR was the rarest.
- One-bit half-adder and controlled-not circuits were successfully implemented using discovered gate architectures.
Conclusions:
- Single actin molecules possess inherent information processing capabilities.
- Actin-based molecular automata can perform fundamental computational tasks.
- The study discusses the speed and space efficiency of F-actin molecular computers.
More Related Videos
Related Concept Videos
Introduction to Actin
6.7K
Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution. Actin coding genes are conserved within species and across...
6.7K
Formation of Higher-order Actin Filaments
3.7K
The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
The high-order actin...
3.7K
Actin Polymerization
8.7K
Actin polymerization occurs through the head-to-tail association of binding sites on monomeric actin or G-actin to form filamentous or F-actin. The polymerization can be divided into three phases ̶ nucleation, elongation, and steady-state phase.
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
The nucleation phase involves forming a stable nucleus consisting of three actin monomers to form a new actin filament. Actin-binding proteins such as formins and Arp2/3 complex help filament growth post-nucleation. The Formins form straight...
8.7K
Generation of Straight or Branched Actin Filaments
3.9K
The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
3.9K
Actin Filament Depolymerization
4.0K
Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
In F-actin, the ADF/cofilin proteins...
4.0K
Actin Polymerization and Cell Motility
6.8K
Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate....
6.8K


