Fluorimetric studies of tryptophyl exposure in concanavalin A

Robert Pelley, Paul Horowitz

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

Studies of the iodide ion quenching of the intrinsic fluorescence of Concanavalin A indicate that 50% of the tryptophyl fluorescence originates from exposed residues. This agrees with the X-ray crystallographic determination that two of the four tryptophan residues in a Concanavalin A monomer are on the surface. Previous studies have indicated that conformational changes induced by sugar binding alter the environment of aromatic residues. The present investigation finds that neither the specific binding of α-methyl-d-mannoside nor alteration of the Concanavalin A quaternary structure changes the number or accessibility of the solvent-exposed tryptophan residues. It therefore appears that the major conformational transitions in Concanavalin A do not affect steric access to the surface tryptophans and the effects previously observed may be ascribed to structurally internal tryptophan residues.

Original languageEnglish (US)
Pages (from-to)359-363
Number of pages5
JournalBBA - Protein Structure
Volume427
Issue number1
DOIs
StatePublished - Mar 18 1976
Externally publishedYes

ASJC Scopus subject areas

  • Medicine(all)

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