Unit

UNIT 11.4 Chemical Cleavage of Proteins in Solution

  1. Dan L. Crimmins1,
  2. Sheenah M. Mische2,
  3. Nancy D. Denslow3

Published Online: 1 JUN 2005

DOI: 10.1002/0471140864.ps1104s40

Current Protocols in Protein Science

Current Protocols in Protein Science

How to Cite

Crimmins, D. L., Mische, S. M. and Denslow, N. D. 2005. Chemical Cleavage of Proteins in Solution. Current Protocols in Protein Science. 41:11.4:11.4.1–11.4.11.

Author Information

  1. 1

    Washington University School of Medicine, St. Louis, Missouri

  2. 2

    Boehringer Ingelheim Pharmaceuticals, Ridgefield, Connecticut

  3. 3

    University of Florida, Gainesville, Florida

Publication History

  1. Published Online: 1 JUN 2005
  2. Published Print: MAY 2005

Abstract

Described in this unit are five basic protocols that are widely used for specific and efficient chemical cleavage of proteins in solution. Cyanogen bromide (CNBr) cleaves at methionine (Met) residues; BNPS-skatole cleaves at tryptophan (Trp) residues; formic acid cleaves at aspartic acid-proline (Asp-Pro) peptide bonds; hydroxylamine cleaves at asparagine-glycine (Asn-Gly) peptide bonds, and 2-nitro-5-thiocyanobenzoic acid (NTCB) cleaves at cysteine (Cys) residues. Because the above loci are at relatively low abundance in most proteins, digestion with these agents will yield relatively long peptides.