Conformations of Purine Ribosyl 5′-Nucleotides Bound to Glycogen Phosphorylase b
作者： Michel MORANGE , Annie KOLB , Henri BUC , Claude CHACHATY , Gerard LANGLET
DOI: 10.1111/J.1432-1033.1977.TB11371.X
关键词:
摘要: The effects of the phosphate ion, glucose 1-phosphate and glycogen on binding several nucleotides to phosphorylase b have been investigated by 1H 2H linewidth measurements electron spin resonance. A graphical method is proposed determine respective contribution strong weak nucleotide sites enzyme H-8, H-2 H-1′. The site governed residence time in case AMP. clAMP IMP ternary complexes with HPO42- transverse relaxation that GMP complex. It shown this latter complex takes an anti conformation instead a syn its binary b. This change related enhanced activity reorientation correlation estimated from 2H-8 found order 10−7 s agreement our previous measurements. The dependence concentrations substrates studied resonance N6-(2,2,6,6-tetramethyl-piperidine-4-yl-1-oxy)-adenosine 5′-monophosphate. proton induced nitroxide group compound indicates distance 1–2 nm between two
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