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Journal of Chemical Physics / Volume 117 / Issue 22 / ARTICLES / Polymers, Biopolymers, and Complex Systems

J. Chem. Phys. 117, 10321 (2002); http://dx.doi.org/10.1063/1.1519239 (8 pages)

Influence of the hydrophobic face width on the degree of association of coiled–coil proteins

Susana Magaña, Ana M. Rubio, and Antonio Rey

Departamento de Química Física, Facultad de Ciencias Químicas, Universidad Complutense, E-28040 Madrid, Spain

(Received 26 June 2002; accepted 12 September 2002)

A very simplistic computational model for the simulation of the association of dimeric coiled–coil proteins has been extended to permit the formation of higher order quaternary structures. The main parameter of the new model is ω, the width of the potential well representing the attraction among hydrophobic residues. For values of ω ranging from 0.5 to 3.0 Å, our Monte Carlo simulations predict the formation of trimers at low temperatures. The different structures (monomers, dimers, and trimers) which populate the simulated system at various temperatures allow us to discuss the optimum value of ω from the point of view of the thermal unfolding transition. On the other hand, the detailed analysis of the trimer structure provides a different point of view about the performance of the model, when compared with the structural information experimentally available for trimeric coiled–coils. © 2002 American Institute of Physics.

© 2002 American Institute of Physics

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KEYWORDS and PACS

Keywords

proteins, molecular biophysics, association, Monte Carlo methods

PACS

  • 87.14.E-

    Proteins

  • 87.15.K-

    Molecular interactions; membrane-protein interactions

  • 82.30.Nr

    Association, addition, insertion, cluster formation

ARTICLE DATA

Digital Object Identifier
http://dx.doi.org/10.1063/1.1519239

PUBLICATION DATA

ISSN

0021-9606 (print)  
1089-7690 (online)

Publisher

$abstract.society.value is a Member of CrossRef American Institute of Physics

For access to fully linked references, you need to log in.
    M. M. Gil, A. M. Rubio, and A. Rey, J. Chem. Phys. 111, 2311 (1999)JCPSA6000111000005002311000001.

    S. G. Prolongo, A. M. Rubio, and A. Rey, J. Chem. Phys. 113, 11343 (2000)JCPSA6000113000024011343000001.


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