File:Amphipathische α-Helix.png

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Deutsch: Das hydrophobe Segment der α-Helix besteht größtenteils aus Aminosäureresten mit unpolaren Seitenketten, die mit dem unpolaren Kern der Lipiddoppelschicht wechselwirken.

Die in die wässrige Phase und den hydrophilen Anteil der Lipiddoppelschicht ragenden Seitenketten sind überwiegend polar.

Aufgrund der daraus resultierenden Amphiphilie sind Transmembranhelices in der Lage, die hydrophoben und hydrophilen Bereiche einer Lipiddoppelschicht zu durchspannen.
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Author Jonas Honold

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Date/TimeThumbnailDimensionsUserComment
current19:31, 1 August 2021Thumbnail for version as of 19:31, 1 August 20218,008 × 7,370 (1,004 KB)Jonas Honold (talk | contribs)Entfernung überschüssiger Ränder
13:10, 1 August 2021Thumbnail for version as of 13:10, 1 August 20218,866 × 8,336 (1.08 MB)Jonas Honold (talk | contribs)Uploaded own work with UploadWizard

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