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Modulating Protein Structure

Creative Biolabs provides custom protein structure modulating services for the design of functional proteins. Powerful computer algorithms and methods have been developed to manipulate protein folding with high controllability and operability.

As we know, the sequence of a protein defines its structure, which in turn decides the function. Protein structure modulation means to design a functional protein by modifying the protein sequence. Therefore, the first step is to design the primary protein sequence for an arbitrary structure with the intended function in mind. To this end, many design algorithms have been focusing on the ability to reliably predict sequences that can fold specifically into desired tertiary structures. This has proven to be a robust tool to understand the forces that govern protein folding. Furthermore, protein structure modulation has been used to increase the stability of biological proteins, adjust their solubility and oligomerization behavior, and produce entirely novel folds.

Figure 1. Schematic representation of the Protein Structures.

Many eukaryotic enzymes use complex glycan structures to assist the protein folding and functions. Allosteric regulation involves the binding an effector molecule at a site other than the enzyme's active site for a conformational change. The effect of such binding can either enhance or decrease the protein's activity. For example, camelid-derived single-domain antibodies (nanobodies) have been used to modulate the conformation and spectral properties of the green fluorescent protein (GFP) in living cells. Lipids, on the other hand, are shown to influence the folding, structure and function of membrane proteins (e.g., the binding of lipids to potassium channels). However, it seems that there are lipids that merely bind the protein, while others modulate the structure and/or function. Phosducin (Pdc) is a highly conserved phosphoprotein, and is important in regulating of G protein signaling, transcriptional control, and modulation of blood pressure. Binding to the 14-3-3 protein causes Pdc to be negatively regulated by phosphorylation, which also leads to notable structural changes.

There could be still many other factors that influence protein structures. Their combined effects can be as important as they are complex. It is therefore not wise to neglect them during the structure modulation. We can simulate your protein structures by taking them into consideration, ensuring the structures to best represent their natural confirmations. If requested, techniques like X-ray crystallography and NMR are also available to experimentally determine the 3D structures too.

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