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New computer simulation helps explain folding in important cellular protein
Date:7/29/2009

. (Wang-Landau, named for David Landau and Fugao Wang, is a Monte Carlo algorithm that has proved to be useful in studying a variety of physical systems. Wang was a doctoral student at UGA and now works for the Intel Corp.)

GpA is a 131-amino acid protein that spans the human red-blood cell membrane and is crucial in cell procedures. Because it has been studied in depth for many years, it also serves as an important model system for how similar systems work. That's why the new simulation may open doors in many other areas of inquiry.

"The main advantage of this two-step approach lies in its flexibility as well as its generality," said Landau. "This method is widely applicable to any study of biological systems, such as the folding process of soluble proteins, polymers, DNA or protein complexes. Therefore, it is an excellent alternative to other simulation methods used traditionally in the field of protein-folding thermodynamics."

In the current study, the team discovered something generally important about membrane proteins in general, too. They found that unlike some proteins for which folding is mainly governed by their attraction to or repulsion by water, the process in GpA is driven by a subtle interplay between multiple types of interactions.


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Contact: David Landau
dlandau@uga.edu
706-542-2908
University of Georgia
Source:Eurekalert

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