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Azidohomoalanine: A Conformationally Sensitive IR Probe of Protein Folding, Protein Structure, and Electrostatics


  • This work was supported by NSF grants CHE 0806433 to D.P.R., CBET 1080909 to I.C. and NIH grant GM053640 to R.B.D. We thank Dr. Lisa Miller and Megan Bourassa from Brookhaven National Laboratory for assistance in collecting preliminary data, and Wenli Meng for his help with the NMR experiments. We also thank Dr. Antonius Kohler from the Stony Brook University Proteomics Center for help with the mass spectrometry. The proteomics center is supported by NIH/NCRR 1 S10 RR025072-1.


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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.