【摘 要】
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Dear Editor,The functional diversity of proteins is related to the cooperation of multiple domains.Independent globular domains are typically joined by a flexib
【机 构】
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Hefei National Laboratory for Physical Science at the Microscale & School of Life Science, Universit
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Dear Editor,The functional diversity of proteins is related to the cooperation of multiple domains.Independent globular domains are typically joined by a flexible length of polypeptide chain,which makes the structural analysis of multi-domain proteins difficult.Here,we describe the combined use of solution NMR (nuclear magnetic resonance) and EPR (electron paramagnetic resonance) for the structural analysis of a protein with two separate domains.The structure of each domain was determined independently using conventional NMR restraints,and the relative orientation of the two separate domains was confined using long-distance restraints obtained by NMR-PRE (paramagnetic relaxation enhancement) and EPR-DEER (double electron-electron resonance,also celled PELDOR:pulsed electron double resonance.
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