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New Principles of Protein Structure: Nests, Eggs—and What Next?
Author(s) -
Pal Debnath,
Sühnel Jürgen,
Weiss Manfred S.
Publication year - 2002
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200290009
Subject(s) - torsion (gastropod) , ion , enantiomer , amino acid , crystallography , nest (protein structural motif) , dihedral angle , partial charge , protein structure , chemistry , computational chemistry , stereochemistry , biology , molecule , zoology , biochemistry , organic chemistry , hydrogen bond
Protein structure prediction, not only description : A step in this direction is the discovery that many anion and cation binding sites (where ions can be atoms exhibiting a full or partial charge) in proteins are made up of three amino acids of which two exhibit “enantiomeric” main‐chain conformations. The combination of torsion angle pairs determines whether an RL or an LR nest is formed (see picture).

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