Structural Implications of Sequence Variability in Immunoglobulins

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1977 Jun 1

PMID 407580

Citations 9

Authors

E A Padlan

Affiliations

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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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