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High resolution nuclear magnetic resonance studies of the conformation and orientation of melittin bound to a lipid-water interface.

Previously, the size and stoichiometry of mixed micelles of perdeuterated dodecylphosphocholine and melittin were characterized and the 1H NMR spin systems of most amino acid residues of micelle-bound melittin identified. One- and two-dimensional 1H-1H Overhauser experiments have now been used to ob...

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Detaylı Bibliyografya
Asıl Yazarlar: Brown, L R, Braun, W, Kumar, A, Wüthrich, K
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: 1982
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC1329145/
https://ncbi.nlm.nih.gov/pubmed/6275926
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