Premium
Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics
Author(s) -
TaskentSezgin Humeyra,
Chung Juah,
Banerjee Partha S.,
Nagarajan Sureshbabu,
Dyer R. Brian,
Carrico Isaac,
Raleigh Daniel P.
Publication year - 2010
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.201003325
Subject(s) - electrostatics , folding (dsp implementation) , protein folding , methionine , chemistry , crystallography , computer science , biochemistry , amino acid , engineering , electrical engineering
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.