UV difference spectroscopy of ligand binding to maltose‐binding protein

FEBS Letters

Gehring, Kalle³  Nikaido, Hiroshi²  Bao, Kogan¹ 

[1] Macromolecular Structure Group, Department of Cell and Molecular Biology, Lawrence Berkeley Laboratory, University of California, Berkeley, CA 94720, USA;Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA;Groupe de Biophysique, Ecole Polytechnique, 91128 Palaiseau, France

关键词: Maltose;    Maltodextrin;    UV difference spectroscopy;    Anomer specificity;    Periplasmic binding protein;    MBP;    maltose-binding protein;    NMR;    nuclear magnetic resonance;    UV;    ultraviolet;   

DOI  :  10.1016/0014-5793(92)80159-E

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We have used UV absorbance spectroscopy to study the binding of linear and circular maltodextrins to maltose-binding protein (MBP). Titrations with maltose yield three ??? points in the difference spectrum of MBP, consistent with two protein conformations: ligand-free and ligand-bound. In contrast, titrations with maltotetraose reveal three conformation: ligand-free, a low-affinity liganded state, and a high affinity liganded state. These results confirm and extend the results from tritium NMR spectroscopy, namely, that MBP can bind maltodextrin either by the sugar's anomeric end (high affinity) or by the middle of the maltodextrin chain flow affinity.

【 授权许可】

Unknown