Monoclinic uncomplexed double-stranded, antiparallel, left-handed beta 5.6-helix (increases decreases beta 5.6) structure of gramicidin A: alternate patterns of helical association and deformation

A comparison of the monoclinic and orthorhombic crystal structures of the uncomplexed double-stranded, antiparallel, left-handed beta-helix (5.6 amino acid residues per turn) (increases decreases beta 5.6) conformers of gramicidin A reveals marked differences in the tryptophan side-chain orientation...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 1991-06, Vol.88 (12), p.5345-5349
Hauptverfasser:	Langs, D A, Smith, G D, Courseille, C, Précigoux, G, Hospital, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Crystallization Gramicidin - chemistry Protein Conformation X-Ray Diffraction
Online-Zugang:	Volltext
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