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. 1977 Jun;74(6):2551–2555. doi: 10.1073/pnas.74.6.2551

Structural implications of sequence variability in immunoglobulins.

E A Padlan
PMCID: PMC432211  PMID: 407580

Abstract

Immunoglobulin sequences were compared by using a technique that takes into account the dissimilarity in physicochemical properties of amino acids. Exterior residues showed greater structural variability than interior residues. High structural variability was found at positions known from crystallographic studies to be involved in hapten binding.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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