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Carboxyl group hydrogen bonding in X‐ray protein structures analysed using neutron studies on amino acids
Author(s) -
Ramanadham M.,
Jakkal V.S.,
Chidambaram R.
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)81339-2
Subject(s) - hydrogen bond , group (periodic table) , amino acid , chemistry , crystallography , x ray , neutron , biochemistry , organic chemistry , molecule , physics , nuclear physics
A method is proposed to make a distinction between ionized and neutral carboxyl groups in X‐ray protein structures. This is based on an analysis of the relative hydrogen bonding populations and bond‐length bond‐valence correlations in high‐precision neutron studies of amino acids and small peptides. With the help of this method, four amino acid residues containing carboxyl groups in the refined structure of triclinic hen egg‐white lysozyme have been analysed. Two of these, Glu‐35 and Asp‐52, are involved in lysozyme function, while the other two, Glu‐7 and Asp‐101, form a protein‐protein inter‐molecular contact in the triclinic structure.