Publications by authors named "Jacob Gah-Kok Gan"
Article Synopsis
- The study examines how homodimer complexes (pairs of identical proteins) are formed and their stability, as well as how they function in biological processes.
- Some homodimers form directly (2-state) while others involve stable intermediate forms (3-state).
- By analyzing 41 different homodimer structures using X-ray crystallography, the research identifies key structural differences that help predict how these complexes fold and interact.
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.
Protein dimer interfaces (homodimer - same polypeptide and heterodimer - different polypeptide) display geometric and chemical properties that give the non-covalent assembly its stability and specificity. Therefore, it is important to understand the molecular principles of dimer interaction. Several studies on homodimer interaction are available.
View Article and Find Full Text PDFProtein subunit dimers are either homodimers (consisting of identical polypeptides) or heterodimers (consisting of different polypeptides). Protein dimers are involved in several cellular processes and an understanding of their molecular principle in complexations (subunit-subunit interaction) is essential. This is generally studied using 3D structures of homodimers and heterodimers determined by X-ray crystallography.
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