Identification of protein oligomerization states by analysis of interface conservation

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SWISS-MODEL: homology modelling of protein structures and complexes (2018, neutral): “The basic assumption is that biologically relevant interfaces are less free to vary than the rest of the protein surface (60,61).”
Protein–protein interaction and quaternary structure (2008, methodology): “…sequences of N homologous proteins, the variability at sequence position i is commonly measured by the Shannon entropy (Sander & Schneider, 1993 ; Elcock & McCammon, 2001 ; Caffrey et al. 2004 ; Guharoy & Chakrabarti, 2005) : s(i)=x X k=1, T pk ln pk (7) pk is the fraction of the sequences that…”
Diffusion, Crowding & Protein Stability in a Dynamic Molecular Model of the Bacterial Cytoplasm (2010, methodology): “The quaternary structure of each selected structure was determined using the PQS web server [80] and was verified, where possible, with the EcoCyc database; it should be noted that correct identification of a protein’s quaternary structure is a non-trivial undertaking, and the PQS predictions are un”
Analysing six types of protein-protein interfaces. (2003, methodology): “One is based on calculating the reduction of solvent accessibility due to oligomerisation(37) and the other is based on measuring the conservation of contacting residues.(38) We used the PQSserver,(37) which applies the first method, to eliminate PDB files that appear to be packing complexes rather ”