ISSN:
1573-3904
Keywords:
α/310-Helix〉
;
Nitroxide amino acid
;
Peptide conformation
;
X-ray diffraction
;
α-Tetrasubstituted amino acids
;
Trichogin
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract An X-ray diffraction analysis of the [Fmoc0,TOAC4,8, Leu-OMe11] analogue of thelipopeptaibol antibiotic trichogin A IV shows that the undecapeptide isfolded in a right-handed, mixed α/310-helix. The helicalmolecules are connected in a head-to-tail arrangement along the b-axisthrough C=O···H-N intermolecular H-bonding. Thispacking mode generates a hydrophobic cavity where the FmocNα-protecting groups are accommodated. The distances andangles between the nitroxide groups of the two TOAC residues, separated byone turn of the α-helix, have been determined.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008874816982
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