Probing Protein Tertiary Structure with Amidination

A chemical derivatization method, amidination, that has recently been effectively employed in peptide mass spectrometry experiments is used to covalently modify lysines in several standard proteins. Protein and peptide mass spectra identify sites at which the reaction does or does not occur. This is...

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Veröffentlicht in:	Analytical chemistry (Washington) 2005-11, Vol.77 (22), p.7274-7281
Hauptverfasser:	Janecki, Dariusz J, Beardsley, Richard L, Reilly, James P
Format:	Artikel
Sprache:	eng
Schlagworte:	Amination Amines - chemistry Amino Acid Sequence Analytical chemistry Animals Carbonic Anhydrase II - chemistry Carbonic Anhydrase II - metabolism Cattle Chemistry Crystallography, X-Ray Cysteine - chemistry Exact sciences and technology Hemoglobins - chemistry Hemoglobins - metabolism Humans Magnetic Resonance Spectroscopy Mass spectrometry Models, Molecular Molecular Sequence Data Peptides Protein folding Protein Structure, Tertiary Proteins - chemistry Proteins - metabolism Solvents Spectrometric and optical methods Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Ubiquitin - chemistry Ubiquitin - metabolism
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Beschreibung
Zusammenfassung:	A chemical derivatization method, amidination, that has recently been effectively employed in peptide mass spectrometry experiments is used to covalently modify lysines in several standard proteins. Protein and peptide mass spectra identify sites at which the reaction does or does not occur. This is therefore a rapid approach to elucidate solvent-accessible regions of folded proteins.
ISSN:	0003-2700 1520-6882
DOI:	10.1021/ac050891z