Binding orientations of α and β methyl D glucopyranoside to concanavalin A as studied by 13C carbon magnetic resonance

Curtis F. Brewer, D. Marcus, A. P. Grollman, H. Sternlicht

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Previous results of various binding properties of concanavalin A (Con A) are presented with specific reference to such binding properties of the protein with bivalent metal ions, and of alpha and beta glucopyranoside sugar derivatives. The authors studied the mechanism of sugar binding to Con A at pH 5.6 by carbon magnetic resonance relaxation measurements of uniformly enriched 14% 13C alpha and beta methyl D glucopyranoside in the presence of Zn2+, Co2+, and Mn2+, transition metal derivatives of the protein. The experimental results are presented in 2 elaborate figures and with 2 sets of tables. Each of these figures and tables is discussed in considerable detail as regards the experimental data and their theoretical interpretation. Literature references are cited. (Hansen - Philadelphia, Pa.)

Original languageEnglish (US)
Pages (from-to)978-988
Number of pages11
JournalAnnals of the New York Academy of Sciences
VolumeVol.222
StatePublished - 1973

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Magnetic resonance
Concanavalin A
Sugars
Magnetic Resonance Spectroscopy
Carbon
Metals
Derivatives
Transition metals
Metal ions
Carrier Proteins
Ions
Proteins
methylglucoside
Protein

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Binding orientations of α and β methyl D glucopyranoside to concanavalin A as studied by 13C carbon magnetic resonance. / Brewer, Curtis F.; Marcus, D.; Grollman, A. P.; Sternlicht, H.

In: Annals of the New York Academy of Sciences, Vol. Vol.222, 1973, p. 978-988.

Research output: Contribution to journalArticle

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AU - Sternlicht, H.

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