The peptide alkaloid anachelin: NMR spectroscopic evidence for β-turn formation in aqueous solution

Chimia

Volumn 58, Issue 4, 2004, Pages 212-214

  Gademann, Karl ^a   Budzikiewicz, Herbert ^b  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITY OF COLOGNE   (Germany)

Author keywords

Anachelin; Conformational analyses; Cyanobacteria; Natural product; NMR spectroscopy; Turn

Indexed keywords

ALKALOID DERIVATIVE; ANACHELIN; IRON; PEPTIDE DERIVATIVE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AQUEOUS SOLUTION; CONFERENCE PAPER; IRON BINDING CAPACITY; METAL BINDING; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

EID: 2442430177     PISSN: 00094293     EISSN: None     Source Type: Journal    
DOI: 10.2533/000942904777677966     Document Type: Conference Paper

References (13)

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13. It is interesting to note that a tetrapeptide (e.g. Asn-Pro-Asp-Met), obviously lacking flanking residues, did not show any sign of β-turn formation, see: X. Liu, P.G. Scott, A. Otter, G. Kotovych, Biopolymers 1992, 32, 119.