Global structure and dynamics of human apolipoprotein CII in complex with micelles: evidence for increased mobility of the helix involved in the activation of lipoprotein lipase

Research describes the three-dimensional global structure of the human apolipoprotein CII-sodium dodecyl sulfate micelle complex for the first time. Data reveal that the C-terminal helix of the enzyme activates lipoprotein lipase and it exhibits a higher degree of internal motion compared to other helices as indicated by the relaxation kinetics.