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EPR spectroscopy, performed after site-directed spin-labeling, was used tostudy structural dynamics in a cold-adapted alkaline phosphatase (EC3.1.1.1). Differences in the structural environment of six spin-labeled sidechains allowed them to be classified (with reference to previously obtainedmobility maps) as belonging to loop positions (either relatively surfaceexposed or in structural contact) or helix positions (surface exposed, incontact, or buried).
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Báo cáo khoa học: Structural features and dynamics of a cold-adapted alkaline phosphatase studied by EPR spectroscopy
