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. 1997 Oct;6(10):2072–2083. doi: 10.1002/pro.5560061003

Ideal architecture of residue packing and its observation in protein structures.

G Raghunathan 1, R L Jernigan 1
PMCID: PMC2143567  PMID: 9336831

Abstract

A simple model of sphere packing has been investigated as an ideal model for long-range interactions for the packing of non-bonded residues in protein structures. By superposing all residues, the geometry of packing around a central residue is investigated. It is found that all residues conform almost perfectly to this lattice model for sphere packing when a radius of 6.5 A is used to define non-bonded (virtual) interacting residues. Side-chain positions with respect to sequential backbone segments are relatively regular as well. This lattice can readily be used in conformation simulations to reduce the conformational space.

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Selected References

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