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Adsorption-induced conformational changes in protein diffusion-aggregation surface assemblies

Hugues Berry 1 Delphine Pellenc 2 Olivier Gallet 2
1 ALCHEMY - Architectures, Languages and Compilers to Harness the End of Moore Years
LRI - Laboratoire de Recherche en Informatique, UP11 - Université Paris-Sud - Paris 11, Inria Saclay - Ile de France, CNRS - Centre National de la Recherche Scientifique : UMR8623
2 ERRMECe - Equipe de recherche sur les relations matrice extracellulaire-cellules
Abstract : Two-dimensional rigid colloid aggregation models may be applied to protein layers when no large conformational change is involved. Yet, following adsorption, several proteins undergo a conformational transition that may be involved in aggregative structures. Our focus here is how a conformational change might influence surface clustering in a diffusion-aggregation model. We propose a model including diffusion, aggregation, and unfolding of proteins that are randomly adsorbed onto a surface. Our model allows simulating the case where protein-protein interaction favors unfolding and the case where this interaction prevents it. We study the effect of a simple disk-to-rod unidirectional unfolding and investigate the morphology of the resulting clusters in the diffusion- and reaction-limited regimes. A rich variety of structures is produced, with fractal dimension differing from that in universal diffusive aggregation models. Increasing unfolding probability shifts the system from the neighbor-induced to the neighbor-prevented unfolding regime. The intermediate structures that arise from our model could be helpful in understanding the assembly of different observed protein structures.
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https://hal.inria.fr/inria-00001064
Contributor : Hugues Berry <>
Submitted on : Monday, January 30, 2006 - 10:27:49 AM
Last modification on : Wednesday, December 2, 2020 - 3:43:13 AM

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  • HAL Id : inria-00001064, version 1

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INRIA | CNRS | UMR8623 | UNIV-CERGY | ERRMECE | I-MAT | CY-TECH-SE

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Hugues Berry, Delphine Pellenc, Olivier Gallet. Adsorption-induced conformational changes in protein diffusion-aggregation surface assemblies. Physical Review E : Statistical, Nonlinear, and Soft Matter Physics, American Physical Society, 2005, 72, pp.051904. ⟨inria-00001064⟩

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