Urea aqueous solution is ubiquitously used to denature protein. Regardless of its
extensive use, the mechanism is still unclear and remains an active field of study. There
have been two proposed mechanisms, the direct and indirect. The indirect mechanism,
which attributes the ability of urea of changing water structure, is susceptible since many
research works show that there is little effect of urea on water structure. The current
study provided evidence for the indirect mechanism by demonstrating that the
introduction of urea slightly changes the water structure in the hydrophobic interfacial
areas.
In the current study, the urea aqueous solution systems with either gas-liquid or
hydrophobic interface are studied by MD simulations, and the structures of water near
the interfacial areas are analyzed in terms of density, orientation and number of
hydrogen bonds. For each kind of interface, systems with four different urea
concentrations are included, ranging from 0M to 8M. The results show slight change of
water structure by the urea solute on the hydrophobic interface in terms of the
orientation and number of hydrogen bonds per water molecule.
| Identifer | oai:union.ndltd.org:tamu.edu/oai:repository.tamu.edu:1969.1/ETD-TAMU-2681 |
| Date | 15 May 2009 |
| Creators | Yu, Meng |
| Contributors | Gao, Yi-Qin |
| Source Sets | Texas A and M University |
| Language | en_US |
| Detected Language | English |
| Type | Book, Thesis, Electronic Thesis, text |
| Format | electronic, application/pdf, born digital |
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