Science News

Scientists Discover The Origin Of A Mysterious Physical Force

ScienceDaily (Mar. 13, 2005) — Ever since the 1970s, scientists have been trying to establish the cause of a repulsive force occurring between different electrostatically charged molecules, such as DNA and other biomolecules, when they are very close to each other in aqueous media. This force became know as hydration force.

Jordi Faraudo, a researcher for the Department of Physics at the Universitat Autònoma de Barcelona, and Fernando Bresme of the Department of Chemistry at Imperial College London have studied this mysterious force in detail and have discovered where its origins lie.

In the same way that a flag flutters in the direction the wind is blowing, at a microscopic level water molecules are gently attracted towards the direction in which an electric field is pointing. However, when the water is in contact with surfaces that create small electric fields, such as chemical compounds like those found in many detergents, this is no longer the case: the water molecules have a remarkable capacity to organise themselves into complex structures that are strongly orientated in such a way as to cancel out the electric field, and on some occasions, to reverse it. This abnormal behaviour was discovered by the same researchers and published in Physical Review Letters in April 2004.

The scientists have now discovered that this strange property is responsible for the hydration force that acts when water is surrounded by certain types of electrostatically charged molecules, such as DNA and some biological compounds, and when thin films form in detergents. The discovery has been published in today's edition of Physical Review Letters.

Water is the solvent in which most physical, chemical and biological processes take place. Therefore, it is essential to understand the nature of interactions between molecules dissolved in water in order to understand many of these processes. Two of the most important of these processes are the adherence of substances to cell membranes and the withdrawal of proteins. Both of these are fundamental in biomedical research, since a substantial part of the process of designing new drugs is based on understanding how substances penetrate cell membranes to enter cells. These drugs are often proteins designed to prevent or strengthen the action of other substances. In these cases, accurately identifying the protein folding is essential, since the form these proteins take on when they fold influences how effectively they are able to act.

Fully understanding the properties of this force that occurs when molecules surrounded by water adhere to each other is also useful in the chemical industry, particularly when involving mechanisms in which colloidal suspensions must be stabilised, such as the mechanisms used to produce paints, cosmetics and food products such as yoghurt and mayonnaise.


Adapted from materials provided by Universitat Autonoma De Barcelona.
APA

MLA

Search ScienceDaily

Number of stories in archives: 44,032

Find with keyword(s):
 
Enter a keyword or phrase to search ScienceDaily's archives for related news topics,
the latest news stories, reference articles, science videos, images, and books.
 

Science Video News


Breakthrough for Breathing

Doctors can now keep patients who are in respiratory care safer with a new kind of ventilator. Ventilator oxygen is completely dry and needs to be. ...  > full story

Breaking News

... from NewsDaily.com

In Other News ...

Copyright Reuters 2008. See Restrictions.

Free Subscriptions

... from ScienceDaily

Get the latest science news with our free email newsletters, updated daily and weekly. Or view hourly updated newsfeeds in your RSS reader:

Feedback

... we want to hear from you!

Tell us what you think of the new ScienceDaily -- we welcome both positive and negative comments. Have any problems using the site? Questions?
Post this page to your favorite social bookmarking site:
close
Include this item in your blog or web site:
close
Cite this article in your essay, paper, or report:
close
Email this page's link to a friend or colleague:
close