Kinetic theory of protein filament growth: Self-consistent methods and perturbative techniques

2014 ◽  
Vol 29 (02) ◽  
pp. 1530002 ◽  
Author(s):  
Thomas C. T. Michaels ◽  
Tuomas P. J. Knowles

Filamentous protein structures are of high relevance for the normal functioning of the cell, where they provide the structural component for the cytoskeleton, but are also implicated in the pathogenesis of many disease states. The self-assembly of these supra-molecular structures from monomeric proteins has been studied extensively in the past 50 years and much interest has focused on elucidating the microscopic events that drive linear growth phenomena in a biological setting. Master equations have proven to be particularly fruitful in this context, allowing specific assembly mechanisms to be linked directly to experimental observations of filamentous growth. Recently, these approaches have increasingly been applied to aberrant protein polymerization, elucidating potential implications for controlling or combating the formation of pathological filamentous structures. This article reviews recent theoretical advances in the field of filamentous growth phenomena through the use of the master-equation formalism. We use perturbation and self-consistent methods for obtaining analytical solutions to the rate equations describing fibrillar growth and show how the resulting closed-form expressions can be used to shed light on the general physical laws underlying this complex phenomenon. We also present a connection between the underlying ideas of the self-consistent analysis of filamentous growth and the perturbative renormalization group.

RSC Advances ◽  
2020 ◽  
Vol 10 (6) ◽  
pp. 3233-3245 ◽  
Author(s):  
Amin Koochaki ◽  
Mohammad Reza Moghbeli ◽  
Sousa Javan Nikkhah ◽  
Alessandro Ianiro ◽  
Remco Tuinier

The self-assembly behaviour of dual-responsive block copolymers and their ability to solubilize the drug doxorubicin is demonstrated using molecular dynamics simulations, coarse-grained force field simulations and self-consistent field theory.


2016 ◽  
Vol 18 (30) ◽  
pp. 20281-20289 ◽  
Author(s):  
Bastien Calmettes ◽  
Nicolas Estrampes ◽  
Christophe Coudret ◽  
Thomas J. Roussel ◽  
Jordi Faraudo ◽  
...  

A STM image of the hexagonal network of tri-adamantyl benzene molecules on Ag(111).


2022 ◽  
Author(s):  
Gaurav Kumar ◽  
Sharmistha Sinha

Bacterial microcompartments are substrate specific metabolic modules that are conditionally expressed in certain bacterial species. These all protein structures have size in the range of 100-150 nm and are formed by the self-assembly of thousands of protein subunits, all encoded by genes belonging to a single operon. The operon contains genes that encode for both enzymes and shell proteins. The shell proteins self-assemble to form the outer coat of the compartment and enzymes are encapsulated within. A perplexing question in MCP biology is to understand the mechanism which governs the formation of these small yet complex assemblages of proteins. In this work we use 1,2-propanediol utilization microcompartments (PduMCP) as a paradigm to identify the factors that drive the self-assembly of MCP proteins. We find that a major shell protein PduBB tend to self-assemble under macromolecular crowded environment and suitable ionic strength. Microscopic visualization and biophysical studies reveal phase separation to be the principle mechanism behind the self-association of shell protein in the presence of salts and macromolecular crowding. The shell protein PduBB interacts with the enzyme diol-dehydratase PduCDE and co-assemble into phase separated liquid droplets. The co-assembly of PduCDE and PduBB results in the enhancement of catalytic activity of the enzyme. A combination of spectroscopic and biochemical techniques shows the relevance of divalent cation Mg2+ in providing stability to intact PduMCP in vivo. Together our results suggest a combination of protein-protein interactions and phase separation guiding the self-assembly of Pdu shell protein and enzyme in solution phase.


2017 ◽  
Vol 19 (9) ◽  
pp. 6707-6720 ◽  
Author(s):  
Xiaomin Wan ◽  
Tong Gao ◽  
Liangshun Zhang ◽  
Jiaping Lin

We theoretically engineer a new scheme, which integrates a permanent field for pattern registration and a dynamic external field for defect annihilation, to direct the self-assembly of block copolymers.


2019 ◽  
Vol 55 (11) ◽  
pp. 1659-1662 ◽  
Author(s):  
Si-Yong Qin ◽  
Wen-Qiang Ding ◽  
Zhi-Wei Jiang ◽  
Xinxiang Lei ◽  
Ai-Qing Zhang

An aligned nanofiber matrix is obtained from the self-assembly of an oligopeptide amphiphile, which can capture the residual dipolar couplings of biomolecules.


Langmuir ◽  
2018 ◽  
Vol 34 (4) ◽  
pp. 1613-1626 ◽  
Author(s):  
O. V. Shavykin ◽  
F. A. M. Leermakers ◽  
I. M. Neelov ◽  
A. A. Darinskii

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