TY - JOUR
T1 - Azidohomoalanine
T2 - A conformationally sensitive IR probe of protein folding protein structure and electrostatics
AU - Taskent-Sezgin, Humeyra
AU - Chung, Juah
AU - Banerjee, Partha S.
AU - Nagarajan, Sureshbabu
AU - Dyer, R. Brian
AU - Carrico, Isaac
AU - Raleigh, Daniel P.
PY - 2010/10/4
Y1 - 2010/10/4
N2 - Highly sensitive: The azido analogue of methionine, azidohomoalanine (see picture), is shown to be a sensitive IR probe of protein structure, folding, and electrostatics, as demonstrated for ribosomal protein NTL9. It can be readily incorporated in to proteins, and the azido frequency is significantly blue-shifted in the thermally unfolded state.
AB - Highly sensitive: The azido analogue of methionine, azidohomoalanine (see picture), is shown to be a sensitive IR probe of protein structure, folding, and electrostatics, as demonstrated for ribosomal protein NTL9. It can be readily incorporated in to proteins, and the azido frequency is significantly blue-shifted in the thermally unfolded state.
KW - Azidohomoalanine
KW - Electrostatics
KW - Infrared spectroscopy
KW - Protein folding
KW - Protein modifications
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U2 - 10.1002/anie.201003325
DO - 10.1002/anie.201003325
M3 - Article
C2 - 20815000
AN - SCOPUS:77957576143
SN - 1433-7851
VL - 49
SP - 7473
EP - 7475
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
IS - 41
ER -