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Chemical Synthesis of a Circular Protein Domain: Evidence for Folding‐Assisted Cyclization
Author(s) -
Camarero Julio A.,
Pavel Joanna,
Muir Tom W.
Publication year - 1998
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/(sici)1521-3773(19980216)37:3<347::aid-anie347>3.0.co;2-5
Subject(s) - folding (dsp implementation) , protein folding , topology (electrical circuits) , function (biology) , chemistry , domain (mathematical analysis) , stereochemistry , biophysics , crystallography , mathematics , combinatorics , biochemistry , biology , engineering , microbiology and biotechnology , mathematical analysis , electrical engineering
Extremely fast cyclization of the linear polypeptide precursor 1 takes place to form 2 . The reaction appears to be assisted by the native fold of 1 , which positions the reactive ends in close proximity. The circular topology has no influence on the folding or function of 2 .