The topography of membrane-bound proteins at atomic resolution is known only in rare cases. [1] Although the primary amino-acid sequence of glycophorin A (GPA), the major sialoglycoprotein of the human erythrocytes, has been known for more than twenty years and was the first membrane protein sequenc
Mid-Membrane Photolabeling of the Transmembrane Domain of Glycophorin A in Phospholipid Vesicles
✍ Scribed by Yoshikatsu Ogawa; Wolfgang Hahn; Philippe Garnier; Nobuaki Higashi; Dominique Massotte; Marie-Hélène Metz-Boutigue; Bernard Rousseau; Junzo Sunamoto; Guy Ourisson; Yoichi Nakatani
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 73 KB
- Volume
- 40
- Category
- Article
- ISSN
- 0044-8249
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract __Ternary mixtures of a high‐melting lipid, a low‐melting lipid, and cholesterol are known to form domains of a liquid‐ordered and a liquid‐disordered phase in bilayer membranes. We prepare giant vesicles from a sphingomyelin/dioleoylphosphocholine/cholesterol mixture and then examine t
A systematic study of the photoalkylation of amino acids by α-coupling products. Methionine was shown to be favoured both in the sense of reactivity as well as product stability. benzophenone, a standard photosensitive probe of biomolecules, was performed addressing for the first time chemo-, Prelim
A more global search method, using fewer assumptions, has been used to predict the structure of the dimeric transmembrane region of the protein glycophorin A. The resulting model significantly differs from that previously determined. In particular, the arrangement between the two transmembrane helic