作者: Brian H Barber , Jeremy P Carver , None
DOI: 10.1016/S0021-9258(19)44047-7
关键词: Relaxation (NMR) 、 Proton 、 Crystallography 、 Kinetic energy 、 Chemistry 、 Crystal structure 、 Stereochemistry 、 Molecule 、 Concanavalin A 、 Folding (chemistry) 、 Binding site
摘要: Abstract The measurement of the proton relaxation rate (1/T1) enhancement (e1*) for concanavalin A (Con A)-Mn2+ complex as a function time following addition Mn2+ indicates pH-dependent structural rearrangement at bound site. excess Ca2+ interrupts this kinetic process and results in reduced time-independent value e1*. further α-methyl-d-glucoside to Con A-Mn2+-Ca2+ also alters observable Using recently published 2 resolution crystal structure A, are interpreted arising from gradual folding loop residues 12 22 over initial binding site (formed by 8, 10, 24) close off free access water molecules.