Monte Carlo study of the molecular mechanisms of surface-layer protein self-assembly

2011 ◽  
Vol 134 (12) ◽  
pp. 125103 ◽  
Author(s):  
Christine Horejs ◽  
Mithun K. Mitra ◽  
Dietmar Pum ◽  
Uwe B. Sleytr ◽  
Murugappan Muthukumar
Keyword(s):  
Monte Carlo ◽  
Surface Layer ◽  
Self Assembly ◽  
Molecular Mechanisms ◽  
Monte Carlo Study ◽  
Surface Layer Protein

scholarly journals A Bacterial Surface Layer Protein Exploits Multi-step Crystallization for Rapid Self-assembly

2019 ◽  
Author(s):  
Jonathan Herrmann ◽  
Po-Nan Li ◽  
Fatemeh Jabbarpour ◽  
Anson C. K. Chan ◽  
Ivan Rajkovic ◽  
...  
Keyword(s):  
Surface Layer ◽  
Self Assembly ◽  
Molecular Mechanisms ◽  
Protein Crystallization ◽  
Crystal Nucleation ◽  
Time Resolved ◽  
Bacterial Surface ◽  
Surface Layer Protein

AbstractSurface layers (S-layers) are crystalline protein coats surrounding microbial cells. S-layer proteins (SLPs) regulate their extracellular self-assembly by crystallizing when exposed to an environmental trigger. However, molecular mechanisms governing rapid protein crystallization in vivo or in vitro are largely unknown. Here, we demonstrate that the C. crescentus SLP readily crystallizes into sheets in vitro via a calcium-triggered multi-step assembly pathway. This pathway involves two domains serving distinct functions in assembly. The C-terminal crystallization domain forms the physiological 2D crystal lattice, but full-length protein crystallizes multiple orders of magnitude faster due to the N-terminal nucleation domain. Observing crystallization using time-resolved electron cryo-microscopy (Cryo-EM) reveals a crystalline intermediate wherein N-terminal nucleation domains exhibit motional dynamics with respect to rigid lattice-forming crystallization domains. Dynamic flexibility between the two domains rationalizes efficient S-layer crystal nucleation on the curved cellular surface. Rate enhancement of protein crystallization by a discrete nucleation domain may enable engineering of kinetically controllable self-assembling 2D macromolecular nanomaterials.Significance StatementMany microbes assemble a crystalline protein layer on their outer surface as an additional barrier and communication platform between the cell and its environment. Surface layer proteins efficiently crystallize to continuously coat the cell and this trait has been utilized to design functional macromolecular nanomaterials. Here, we report that rapid crystallization of a bacterial surface layer protein occurs through a multi-step pathway involving a crystalline intermediate. Upon calcium-binding, sequential changes occur in the structure and arrangement of the protein, which are captured by time-resolved small angle x-ray scattering and transmission electron cryo-microscopy. We demonstrate that a specific domain is responsible for enhancing the rate of self-assembly, unveiling possible evolutionary mechanisms to enhance the kinetics of 2D protein crystallization in vivo.

scholarly journals Monte Carlo Study of the Molecular Mechanisms of S-Layer Protein Self-Assembly

2011 ◽  
Vol 100 (3) ◽  
pp. 386a
Author(s):  
Christine Horejs ◽  
Mithun K. Mitra ◽  
Dietmar Pum ◽  
Uwe B. Sleytr ◽  
Murugappan Muthukumar
Keyword(s):  
Monte Carlo ◽  
Self Assembly ◽  
Molecular Mechanisms ◽  
Monte Carlo Study

scholarly journals A Monte Carlo Study of the Self-Assembly of Bacteriorhodopsin

2002 ◽  
Vol 83 (4) ◽  
pp. 1902-1916 ◽  
Author(s):  
Kamakshi Jagannathan ◽  
Rakwoo Chang ◽  
Arun Yethiraj
Keyword(s):  
Monte Carlo ◽  
Self Assembly ◽  
Monte Carlo Study ◽  
The Self

Monte Carlo Study of the Self-Assembly of Achiral Bolaform Amphiphiles into Helical Nanofibers

Langmuir ◽  
2010 ◽  
Vol 26 (5) ◽  
pp. 2979-2982 ◽  
Author(s):  
M. Wahab ◽  
P. Schiller ◽  
R. Schmidt ◽  
H.-J. Mögel
Keyword(s):  
Monte Carlo ◽  
Self Assembly ◽  
Monte Carlo Study ◽  
The Self

Self-assembly of ABC triblock copolymers under 3D soft confinement: a Monte Carlo study

Soft Matter ◽  
2016 ◽  
Vol 12 (3) ◽  
pp. 965-972 ◽  
Author(s):  
Nan Yan ◽  
Yutian Zhu ◽  
Wei Jiang
Keyword(s):  
Monte Carlo ◽  
Self Assembly ◽  
Triblock Copolymers ◽  
Monte Carlo Study ◽  
Abc Triblock Copolymers

A serious of novel morphologies obtained by self-assembly of ABC triblock copolymers under 3D soft confinement.

scholarly journals Effect of Surface Roughness on Aggregation of Polypeptide Chains: A Monte Carlo Study

Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 596
Author(s):  
Nguyen Truong Co ◽  
Mai Suan Li
Keyword(s):  
Surface Roughness ◽  
Self Assembly ◽  
Molecular Mechanisms ◽  
Monte Carlo Study ◽  
The Self ◽  
Living Organisms ◽  
Polypeptide Chains ◽  
The Impact ◽  
Kinetics Of

The self-assembly of amyloidogenic peptides and proteins into fibrillar structures has been intensively studied for several decades, because it seems to be associated with a number of neurodegenerative diseases, such as Alzheimer’s and Parkinson’s disease. Therefore, understanding the molecular mechanisms of this phenomenon is important for identifying an effective therapy for the corresponding diseases. Protein aggregation in living organisms very often takes place on surfaces like membranes and the impact of a surface on this process depends not only on the surface chemistry but also on its topology. Our goal was to develop a simple lattice model for studying the role of surface roughness in the aggregation kinetics of polypeptide chains and the morphology of aggregates. We showed that, consistent with the experiment, an increase in roughness slows down the fibril formation, and this process becomes inhibited at a very highly level of roughness. We predicted a subtle catalytic effect that a slightly rough surface promotes the self-assembly of polypeptide chains but does not delay it. This effect occurs when the interaction between the surface and polypeptide chains is moderate and can be explained by taking into account the competition between energy and entropy factors.

Self-Assembly of Heteroarm Star Copolymers – A Monte Carlo Study

2007 ◽  
Vol 16 (4) ◽  
pp. 386-398 ◽  
Author(s):  
Jitka Havránková ◽  
Zuzana Limpouchová ◽  
Miroslav Štěpánek ◽  
Karel Procházka
Keyword(s):  
Monte Carlo ◽  
Self Assembly ◽  
Monte Carlo Study ◽  
Star Copolymers
Sign in / Sign up

Export Citation Format

Share Document