Document Detail


Toward the description of electrostatic interactions between globular proteins: potential of mean force in the primitive model.
MedLine Citation:
PMID:  17824765     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Monte Carlo simulations are used to calculate the exact potential of mean force between charged globular proteins in aqueous solution. The aim of the present paper is to study the influence of the ions of the added salt on the effective interaction between these nanoparticles. The charges of the model proteins, either identical or opposite, are either central or distributed on a discrete pattern. Contrarily to Poisson-Boltzmann predictions, attractive, and repulsive direct forces between proteins are not screened similarly. Moreover, it has been shown that the relative orientations of the charge patterns strongly influence salt-mediated interactions. More precisely, for short distances between the proteins, ions enhance the difference of the effective forces between (i) like-charged and oppositely charged proteins, (ii) attractive and repulsive relative orientations of the proteins, which may affect the selectivity of protein/protein recognition. Finally, such results observed with the simplest models are applied to a more elaborate one to demonstrate their generality.
Authors:
Vincent Dahirel; Marie Jardat; Jean-François Dufrêche; Pierre Turq
Related Documents :
19441845 - Efforts toward developing probes of protein dynamics: vibrational dephasing and relaxat...
22548785 - Identification of a skp1-like protein interacting with sfb, the pollen s determinant of...
22444585 - We see the light: chemical-genetic protein regulation.
10798525 - A new approach for the calculation of the energy of van der waals interactions in macro...
3031425 - Increase in s-100b protein content in thyroid carcinoma.
3447175 - Continuous compact protein domains.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Journal of chemical physics     Volume:  127     ISSN:  0021-9606     ISO Abbreviation:  J Chem Phys     Publication Date:  2007 Sep 
Date Detail:
Created Date:  2007-09-10     Completed Date:  2007-11-13     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  0375360     Medline TA:  J Chem Phys     Country:  United States    
Other Details:
Languages:  eng     Pagination:  095101     Citation Subset:  IM    
Affiliation:
Université Pierre et Marie Curie-Paris 6, Laboratoire Liquides Ioniques et Interfaces Chargées, UMR CNRS 7612, Case Courrier 51, 4 Place Jussieu 75005 Paris, France. dahirel@ccr.jussieu.fr
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Binding Sites
Computer Simulation
Models, Chemical*
Models, Molecular*
Protein Binding
Proteins / chemistry*
Static Electricity
Stress, Mechanical
Chemical
Reg. No./Substance:
0/Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Contact measurement of internal fluid flow within poly(n-isopropylacrylamide) gels.
Next Document:  Protein elasticity determined by pressure tuning of the tyrosine residue of ubiquitin.