TY - JOUR
T1 - Protein semisynthesis and expressed protein ligation
T2 - Chasing a protein's tail
AU - Schwarzer, Dirk
AU - Cole, Philip A.
PY - 2005/12/1
Y1 - 2005/12/1
N2 - The adaptation of native chemical ligation to protein semisynthesis has become a powerful way to address problems in the analysis of protein structure and function. In particular, the exploitation of nature's inteins in expressed protein ligation is now a standard approach in the study of proteins. Site-specific incorporation of unnatural amino acids, biophysical probes and post-translational modifications in proteins have led to new insights into enzyme mechanisms, protein folding, ion channel function, translation and signaling.
AB - The adaptation of native chemical ligation to protein semisynthesis has become a powerful way to address problems in the analysis of protein structure and function. In particular, the exploitation of nature's inteins in expressed protein ligation is now a standard approach in the study of proteins. Site-specific incorporation of unnatural amino acids, biophysical probes and post-translational modifications in proteins have led to new insights into enzyme mechanisms, protein folding, ion channel function, translation and signaling.
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U2 - 10.1016/j.cbpa.2005.09.018
DO - 10.1016/j.cbpa.2005.09.018
M3 - Review article
C2 - 16226484
AN - SCOPUS:27744495195
SN - 1367-5931
VL - 9
SP - 561
EP - 569
JO - Current Opinion in Chemical Biology
JF - Current Opinion in Chemical Biology
IS - 6
ER -