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Circular-dichroism and fluorescence studies on melittin: effects of C-terminal modifications on tetramer formation and binding to phospholipid vesicles.
Studies were performed on a series of melittin analogues with selective alterations to the positively charged amino acid sequence at the C-terminus. Fluorescence studies were undertaken using the sole tryptophan residue in the analogues as an intrinsic fluorescence probe for indications of tetramer...
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| Hlavní autoři: | , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
1995
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1136327/ https://ncbi.nlm.nih.gov/pubmed/7848277 |
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