Format:
Online-Ressource (PDF-Datei: 130 S., 19.366 KB)
,
Ill., graph. Darst
Content:
Aquaporins are protein channels responsible for the permeation of water and other small solutes through biological membranes in response to osmotic pressure. The goal of the present thesis is to expand our understanding on the molecular machinery of aquaporins by employing molecular dynamics simulations and related computational techniques. First, we provide a solute permeation mechanism for the solute permeation through the Plasmodium falciparum aquaglyceroporin that is a promising antimalarial drug target. In this mechanism, hydrophobic regions in the middle of the channel are the main water rate limiting barriers. In addition, the replacement of water-arginine interactions by solute-arginine interactions and the matching of the solute at the most constricted region of the channel are the main determinants underlying selectivity for the permeation of solutes like glycerol and urea ...
Note:
Göttingen, Univ., Diss., 2011
Additional Edition:
Erscheint auch als Druck-Ausgabe Aponte-Santamaria, Camilo Andrés Understanding the molecular machinery of aquaporins through molecular dynamics simulations 2011
Language:
English
Keywords:
Hochschulschrift
URN:
urn:nbn:de:gbv:7-webdoc-3294-7
URL:
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