Science Sub-Journal: New methods to understand protein dynamics and cell process regulation

Cellular processes are regulated by the balance between different protein shapes, which give these molecules active or inactive functions
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In the complexity of cell regulation, the preferred shape (or conformation) of a protein often depends on its binding to another molecule (called an effector).

Researchers at the Barcelona IRB Molecular Modeling and Bioinformatics Laboratory, led by Dr.
Modesto Orozco, have developed a new computational program that can discover and quantify the shape of functional proteins, thereby revealing the molecular details of cellular processes
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The focus of this work is on proteins under allosteric regulation, which means that their shape changes occur in regions away from the binding site of the effect

Using this method, scientists have studied the regulation of adenylate cyclase (AC), a key enzyme involved in the control of a variety of cellular processes, including regulating the action of a variety of hormones and regulating energy metabolism
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This work reveals a surprisingly simple on/off adjustment of the dynamics of the communication function

Dr.
Orozco explained: “The method we propose can be used to better understand the regulation process of any cellular pathway under allosteric regulation (most of them), and has a profound impact on pharmaceutical and biotechnology applications
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” Also Barcelona Senior professor at the University School of Biology

Based on previous research on co-evolution information

The newly proposed method is based on previous work in molecular modeling and bioinformatics laboratories, focusing on co-evolving information
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Multiple sequence alignments can be used to track the evolutionary history of proteins, and can detect co-evolving amino acid positions, and then use this information to search for natural and alternative protein structures

Dr.

DOI 10.

Probing allosteric regulations with coevolution-driven molecular simulations