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Updated: Jul 31, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Protein domain interfaces: characterization and comparison with oligomeric protein interfaces.
S Jones1, A Marin, J M Thornton
1Biomolecular Structure and Modelling Unit, Department of Biochemistry and Molecular Biology, University College, Gower Street, London WC1E 6BT, UK. sue@biochem.ucl.ac.uk
Protein domain interactions within single molecules share physical and chemical properties with interactions between separate protein molecules. This suggests common principles govern protein assembly and folding.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Science
Background:
- Protein structures are often composed of multiple domains.
- Understanding domain-domain interactions is crucial for protein function and folding.
Purpose of the Study:
- To analyze the physical and chemical properties of intra-chain domain-domain interactions.
- To compare these properties with inter-chain protein-protein interactions.
Main Methods:
- Analysis of two-domain protein structures from the CATH database.
- Calculation of interface properties: size, polarity, hydrogen bonding, and packing.
- Comparison with interface parameters from protein-protein complexes.
Main Results:
- Intra-chain domain interfaces exhibit remarkable similarity to inter-chain interfaces.
- Interface properties are often intermediate between permanent and non-obligate protein complexes.
- Hydrophobic and arginine residues are key components of domain interfaces.
Conclusions:
- Domain-domain interactions share common biophysical principles regardless of whether they are intra- or inter-chain.
- Findings offer insights into protein folding mechanisms and the phenomenon of domain swapping.
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