Deeper insights into protein folding

Jun 26, 2014
Deeper insights into protein folding

Investigating the structure and dynamics of so-called Meso-Bio-Nano (MBN) systems—micron-sized biological or nanotechnology entities—is a rapidly expanding field of science. Now, scientists Alexander Yakubovich and Andrey Solov'yov from MBN Research Centre in Frankfurt, Germany, have produced a new theoretical study of a protein macromolecule changing from a coil structural conformation to a globular one. Their statistic mechanics model, just published in the European Physical Journal D, describes the thermodynamic properties of real proteins in an aqueous environment, using a minimal number of free physical parameters.

In this work, the authors confirmed the validity of their theoretical calculation of dependencies of the protein heat capacities on temperature by comparing it with the corresponding experimental measurements for two proteins, namely an enzyme called staphylococcal nuclease and an oxygen and iron carrier protein called metmyoglobin. Sudden changes in temperature could result in the loss of a protein's three-dimensional structure and function. Thus, these findings could contribute to our understanding of high-energy ions therapy on biological cells.

In this work, the authors focus on the folding and unfolding of globular proteins at various levels of temperature in an aqueous environment. Their statistical mechanics model is inspired by a pre-existing model of solvation of hydrophobic hydrocarbons. This leads to establishing the so-called partition function of this in water environment. In turn, this helps to determine all of the 's thermodynamic characteristics at equilibrium. These include its heat capacity and the average number of amino acids in an unfolded conformation.

The study validates the use of an approximation of three stages of macromolecular complexes undergoing folding and unfolding transformations, instead of using fitting parameters as previously done. These results also significantly expand the possibilities of quantitative description of the structure conformation processes for other proteins obeying simple folding kinetics and complex multi-domain proteins with peculiar folding profiles.

Explore further: Researchers discover new mechanism of DNA repair

More information: A. V. Yakubovich and A. V. Solov'yov (2014), Quantitative thermodynamic model for globular protein folding, European Physical Journal D, DOI: 10.1140/epjd/e2014-50097-3

Related Stories

Predicting protein binding sites on DNA

Oct 15, 2012

In silico prediction of protein folding has the potential to reveal the specificity of a given protein sequence for DNA. Such methods are particularly promising as they could open the road to the rational ...

Quantifying protein-folding mechanisms

Oct 15, 2012

European scientists are investigating the mechanisms by which proteins fold to form complex configurations using single-molecule experimental techniques.

Recommended for you

Researchers discover new mechanism of DNA repair

14 hours ago

The DNA molecule is chemically unstable giving rise to DNA lesions of different nature. That is why DNA damage detection, signaling and repair, collectively known as the DNA damage response, are needed.

Stopping Candida in its tracks

Jul 03, 2015

Scientists are one step closer to understanding how a normally harmless fungus changes to become a deadly infectious agent.

New technique maps elusive chemical markers on proteins

Jul 02, 2015

Unveiling how the 20,000 or so proteins in the human body work—and malfunction—is the key to understanding much of health and disease. Now, Salk researchers developed a new technique that allows scientists ...

User comments : 0

Please sign in to add a comment. Registration is free, and takes less than a minute. Read more

Click here to reset your password.
Sign in to get notified via email when new comments are made.