Structural implications of sequence variability in immunoglobulins.
AUTOR(ES)
Padlan, E A
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=432211Documentos Relacionados
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