Abstract
Complexes of Con A with α- d-glycosides were studied using 11H-NMR, ESR and fluorescence methods. Correlation times,τ c, for the interaction of the aglycon protons with the manganese ion, present at the S1 site of the protein, were calculated from T 1 measurements at two frequencies. The protons of aromatic aglycons have τ c values comparable to the rotational correlation time of the protein molecule, whereas those of non-aromatic aglycons have τ cS 10 to 100 times lower. The correlation times were combined with the experimentally acquired paramagnetic contributions to proton relaxation due to the presence of the manganese ion to yield manganese-proton distances. These distances show that aromatic aglycons bave additional favorable contacts with the protein which stabilize the lectin-saccharide interaction. The results are compared to the crystal structure of the methyl α- d-glycopyranoside complex with Con A and to models earlier proposed for the binding of monosaccharides to Con A.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
