AI Article Synopsis
- Protein dimers can be categorized as homodimers (identical monomers) or heterodimers (non-identical monomers) and play essential roles in processes like catalysis and regulation.
- Understanding these interactions is challenging due to the complex geometry and chemistry of proteins, but researchers rely on 3D structural data from X-ray crystallography to study them.
- The article highlights key differences between homodimer and heterodimer interfaces by examining a select group of significant physical and chemical properties that influence these dimer interactions.
Article Abstract
Protein dimers are either homodimers (complexation of identical monomers) or heterodimers (complexation of non-identical monomers). These dimers are common in catalysis and regulation. However, the molecular principles of protein dimer interactions are difficult to understand mainly due to the geometrical and chemical characteristics of proteins. Nonetheless, the principles of protein dimer interactions are often studied using a dataset of 3D structural complexes determined by X-ray crystallography. A number of physical and chemical properties govern protein dimer interactions. Yet, a handful of such properties are known to dominate protein dimer interfaces. Here, we discuss the differences between homodimer and heterodimer interfaces using a selected set of interface properties.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1891636 | PMC |
| http://dx.doi.org/10.6026/97320630001028 | DOI Listing |
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