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Proteins from the D ‐Chiral World
Author(s) -
Jung Günther
Publication year - 1992
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199214571
Subject(s) - enantiomer , enzyme , protease , chemistry , substrate specificity , protein tertiary structure , stereochemistry , amino acid , biochemistry , computational biology , biology
The chiroptical properties and substrate specificity of the D ‐enantiomer of the naturally occurring HIV protease synthesized by Kent et al. demonstrate that the three‐dimensional structures of D ‐ and L ‐enzymes really are mirror images of one another—that is, identical amino acid sequences actually fold in the same way in the tertiary structure. Interest in D ‐proteins goes beyond basic research, as the enzymatic stability may allow important medical applications; additional areas of application include protein crystallography.
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