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Riding the lipid tides

This presentation by David Stopar, conducted from March to May 2003, dives into the complex interactions and properties of various phosphatidylcholine (PC) lipids and their mutants within DOPC. Caution is advised as the results and models may be premature and insufficiently analyzed, potentially leading to systemic effects if digested or ingested. Key topics include the structural domains of major coat proteins, phase transitions of different PCs, fluorescence studies, and the effects of different solvents on protein behavior. Your cooperation and assistance in this exploration are greatly appreciated.

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Riding the lipid tides

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  1. Riding the lipid tides David Stopar Wageningen, March-May 2003

  2. CAUTION!!! THE RESULTS AND MODELS PRESENTED HERE MAY BE PREMATURED AND UNSUFICIENTLY ANALISED. DIGESTION OF THESE RESULTS MAY LEAD TO SYSTEMIC EFFECTS. PRECAUTION: Avoid ingestion and digestion of this presentation

  3. PC14 1; 9-cis-tetradecenoic PC16 1; 9-cis-hexadecenoic PC18 1; 9-cis-octadecenoic PC20 1; 11-cis-eicosenoic PC22 1; 13-cis-docosenoic Different PC’s

  4. Different mutants in DOPC

  5. Major coat protein structural domains 1-5 N-terminus 6-16 amphiphatic helix 17-23 loop 24-46 transmembrane helix 47-50 C-terminus

  6. Different mutants in PC14 and PC22

  7. Different mutants in PC14 and PC22

  8. CD spectra of major coat protein in different PC’c

  9. I39C mutant in a binary mixture of PC14 and PC22

  10. Spin labeled T46C in different PC14/PC18 mixtures

  11. Phase transitions of different PC’s

  12. Trp26 and BADAN T46C fluorescence in different PC’s

  13. Quenching studies

  14. T46C reconstituted in different PC’s

  15. A49C reconstituted in PC14 and PC22

  16. Major coat protein in UREA, Cholate, SDS and TFE

  17. Different mutants in different solvents

  18. That’s all we had time for, folks! Thanks very much for your help and cooperativity. Cheers, David

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