Argonne Analysis Shows Surprising Activity in Proteins
Research conducted at the US Department of Energy’s Argonne National Laboratory has produced some surprising information about the activities of proteins. Their discoveries could offer cancer researchers important new clues about how these crucial molecules interact with oncology drugs and other medicines.
For over one hundred years, standard models of protein behavior have portrayed them as inflexible locks that only interact with equally rigid molecular keys. Now Argonne’s Advanced Photon Source has shown conformations in five common proteins are much more dynamic than biochemists previously estimated — and they’re strongly influenced by environmental conditions.
Using a new approach which relies on intense x-ray beams, the scientists studied protein interactions in solutions with concentrations of protein molecules varying from 1 to 30 percent. Their investigation revealed the proteins not only had a greater range of motion than expected, they also had the ability to contort themselves into many more configurations in diluted solutions. One part of their examination determined the protein hemoglobin flipped to different conformations based on the accessibility of oxygen in the solution.
Because proteins play a key role in virtually every function of living organisms including metabolism, these findings could prove beneficial to cancer studies investigating how proteins impact treatment efficacy.
If you’d like to learn more, Argonne’s study has been published in the January 11, 2008, edition of the Journal of Molecular Biology.
Source: Argonne National Laboratory News
Related Links: sciencenewsdaily.org; PhysOrg.com; Human Protein Reference Database
Related Podcast: Computational analysis of human protein interaction networks from PROTEOMICS Podcast
Tags: pharmacokinetics; pharmacodynamics; pharmacology; biomolecular chemistry; Illinois Institute of Technology; Illinois; synchrotron
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