TY - JOUR
T1 - Magnetic resonance relaxation of 1H and 17O in aqueous solutions of concanavalin A
AU - Meirovitch, E.
AU - Joseph Kalb, A.
PY - 1973/4/20
Y1 - 1973/4/20
N2 - We have studied the nuclear magnetic resonance relaxation times of 1H and 17O nuclei in aqueous solutions of Mn2+ complexes of concanavalin A. The results indicate that the Mn2+ is coordinated to one exchangeable water molecule. The mean residence time, τh, of this water molecule at the Mn2+ is approximately 1 · 10-7 s in Mn2+-concanavalin A and is ten times as long in Mn2+, Ca2+-concanavalin A. No changes occur on binding of α-methyl glucoside, or on raising the pH to a value where molecular aggregation occurs. It is possible that on occupation of the Ca2+-binding site, the immediate electronic environment of the Mn2+ alters and thus affects the mean residence time of the water molecule. It is also possible that the increase in τh is brought about by restrictions imposed on the exchange of water molecules between bulk solvent and the Mn2+.
AB - We have studied the nuclear magnetic resonance relaxation times of 1H and 17O nuclei in aqueous solutions of Mn2+ complexes of concanavalin A. The results indicate that the Mn2+ is coordinated to one exchangeable water molecule. The mean residence time, τh, of this water molecule at the Mn2+ is approximately 1 · 10-7 s in Mn2+-concanavalin A and is ten times as long in Mn2+, Ca2+-concanavalin A. No changes occur on binding of α-methyl glucoside, or on raising the pH to a value where molecular aggregation occurs. It is possible that on occupation of the Ca2+-binding site, the immediate electronic environment of the Mn2+ alters and thus affects the mean residence time of the water molecule. It is also possible that the increase in τh is brought about by restrictions imposed on the exchange of water molecules between bulk solvent and the Mn2+.
UR - http://www.scopus.com/inward/record.url?scp=0015930748&partnerID=8YFLogxK
U2 - 10.1016/0005-2795(73)90355-3
DO - 10.1016/0005-2795(73)90355-3
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C2 - 4710230
AN - SCOPUS:0015930748
SN - 0005-2795
VL - 303
SP - 258
EP - 263
JO - BBA - Protein Structure
JF - BBA - Protein Structure
IS - 2
ER -