Formation of Protein Charge Ladders by Acylation of Amino Groups on Proteins

@inproceedings{Sgttol1997FormationOP,
  title={Formation of Protein Charge Ladders by Acylation of Amino Groups on Proteins},
  author={Ian J. Sgttol and Janelle R. Anderson and Jinming Gao and Robert G. Chapman and Lyle Isaacs and George I I. lVhitesides},
  year={1997}
}
The values of charge and electrophoretic mobility of a protein are changed upon acylation of its Rand Lys -NH3 groups. Partial acylation of the amino groups of a protein results in a set of derivatives that is often resolved by capillary electrophoresis into a set of distinct peakssthe “rungs” of a protein charge laddersthat differ incrementally in the number of residues modified. Proteins that have values of MW < 50 kD usually form resolved charge ladders when allowed to react with acetic… CONTINUE READING

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  • C. Roberts, E. Córdova, G. M. Unpublished Whitesides, J. R. Anderson, I. J. Colton, G. M. Whitesides

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