Sequence specific 1H-NMR assginments and secondary structure of a carboxy-terminal functional fragment of apolipoprotein CII
In: European journal of biochemistry (Print), Jg. 205 (1992), Heft 1, S. 223-231
Online
academicJournal
- print, 1/2 p
Zugriff:
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.
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Sequence specific 1H-NMR assginments and secondary structure of a carboxy-terminal functional fragment of apolipoprotein CII
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Autor/in / Beteiligte Person: | LYCKSELL, P.-O ; ÖHMAN, A ; BENGTSSON-OLIVECRONA, G ; JOHANSSON, L. B.-Å ; WIJMENGA, S. S ; WERNIC, D ; GRÄSLUND, A |
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Zeitschrift: | European journal of biochemistry (Print), Jg. 205 (1992), Heft 1, S. 223-231 |
Veröffentlichung: | Oxford: Blackwell, 1992 |
Medientyp: | academicJournal |
Umfang: | print, 1/2 p |
ISSN: | 0014-2956 (print) |
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