Document Detail

Aggregation of non-polar solutes in water at different pressures and temperatures: The role of hydrophobic interaction.
MedLine Citation:
PMID:  23039616     Owner:  NLM     Status:  Publisher    
Due to the importance of the hydrophobic interaction in protein folding, we decided to study the effect of pressure and temperature on the phase transitions of non-polar solutes in water, and thereby their solubility, using molecular dynamics simulations. The main results are: (1) within a certain range, temperature induces the aggregation of Lennard-Jones particles in water; and (2) pressure induces disaggregation of the formed clusters. From the simulated data, a non-monotonic coexistence curve for the binary system was obtained, from which a critical point of T(c) = 383 ± 9 K and p(c) = 937 ± 11 bar was determined. The results are in accordance with previous experimental evidence involving transitions of hydrocarbons in water mixtures, and protein unfolding.
C Gastón Ferrara; Osvaldo Chara; J Raúl Grigera
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Publication Detail:
Journal Detail:
Title:  The Journal of chemical physics     Volume:  137     ISSN:  1089-7690     ISO Abbreviation:  J Chem Phys     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0375360     Medline TA:  J Chem Phys     Country:  -    
Other Details:
Languages:  ENG     Pagination:  135104     Citation Subset:  -    
Instituto de Física de Líquidos y Sistemas Biológicos (IFLYSIB) CONICET-UNLP, 59-789, B1900 La Plata, Argentina.
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