Sequence specific 1H‐NMR assignments and secondary structure of a carboxy‐terminal functional fragment of apolipoprotein CII

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Abstract
The structural properties of a synthetic fragment of human apolipoprotein CII (apoCII) has been studied by circular dichroism and proton nuclear magnetic resonance. The fragment corresponds to the carboxy‐terminal 30 amino acid residues and retains the ability of apoCII to activate lipoprotein lipase. Like native apoCII, the fragment has a tendency to self‐associate in pure aqueous solution. Addition of 1,1,1,3,3,3‐hexafluoro‐2‐isopropanol to aqueous solvent dissolves the aggregates and leads to an increase in the α‐helical content of the peptide, probably by stabilizing transient helical structures. The resonances in the 1H‐NMR spectrum of the fragment in 35% (CF3)2CHOH were assigned through standard procedures from nuclear Overhauser enhancement spectroscopy, correlated spectroscopy and total correlated spectroscopy experiments. The NMR data indicates the formation of a stable α helix spanning Ile66–Gly77. Another α helical turn may be formed between Lys55 and Ala59 and possibly span even further towards the carboxyl terminus. These structural elements are different from those previously predicted for this part of the sequence of apoCII.