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Structural Implications of Sequence Variability in Immunoglobulins

Eduardo A. Padlan
Proceedings of the National Academy of Sciences of the United States of America
Vol. 74, No. 6 (Jun., 1977), pp. 2551-2555
Stable URL: http://www.jstor.org/stable/66869
Page Count: 5
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Structural Implications of Sequence Variability in Immunoglobulins
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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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