Assignment of cysteine and tryptophan residues during protein sequencing: Results of ABRF-94SEQ

Jay Gambee, Philip C. Andrews, Karen DeJongh, Greg Grant, Barbara Merrill, Sheenah Mische, John Rush

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Routine assignment of cysteine and tryptophan residues is necessary for completeness of protein sequencing, because cysteine residue provides the major covalent cross-linkage in proteins and contributes to the biological and catalytic activity of many folded polypeptides. While, accurate assignment of tryptophan residues is crucial, when sequencing is used to design oligonucleotide probes of limited redundancy. This chapter discusses methods to improve the reliability of cysteine and tryptophan assignment, and describes the results of ABRF-94SEQ. ABRF-94SEQ allows to see which methods are used successfully in other facilities, and also provide the opportunity to assess these methods. It is observed that some who alkylate and some who does not alkylate, take risks making positive assignments for cysteine, when no PTH-residue or dehydroalanine/DTT adduct is apparent. If this assumption is done, it must be noted that this is not a positive assignment. Although cysteine and tryptophan identification may be problematic, the data suggest that routine identification of these residues should be possible for the majority of facilities.

Original languageEnglish
Pages (from-to)209-217
Number of pages9
JournalTechniques in Protein Chemistry
Volume6
Issue numberC
DOIs
StatePublished - Jan 1 1995

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