CRYSTALLOGRAPHIC STUDY ON HIGHLY STABLE HUMAN INSULINS(Ⅱ)——CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDY OF A21-GLY MUTANT

Ⅰ. INTRODUCTIONThe chemical stability of human insulin preparations is directly related to the residue of A21-Asn at C-terminal of A chain and can be distinctly increased by substituting the A21 residue in the way of protein engineering. Studying the fine three-dimensional structures of

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Veröffentlicht in:中国科学通报:英文版 1992 (15), p.1302-1305
1. Verfasser: 金雷 黄伟军 张英 王大成 L. LANGKJAER J. MARKUSSEN
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description Ⅰ. INTRODUCTIONThe chemical stability of human insulin preparations is directly related to the residue of A21-Asn at C-terminal of A chain and can be distinctly increased by substituting the A21 residue in the way of protein engineering. Studying the fine three-dimensional structures of
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INTRODUCTIONThe chemical stability of human insulin preparations is directly related to the residue of A21-Asn at C-terminal of A chain and can be distinctly increased by substituting the A21 residue in the way of protein engineering. Studying the fine three-dimensional structures of</abstract></addata></record>
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subjects A21-Gly
crystallization
high
human
insulin
mutant
stability
title CRYSTALLOGRAPHIC STUDY ON HIGHLY STABLE HUMAN INSULINS(Ⅱ)——CRYSTALLIZATION AND PRELIMINARY CRYSTALLOGRAPHIC STUDY OF A21-GLY MUTANT
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