ABSTRACT
The basics-focus principle is proposed as a foundation for uses of phages in nanomedicine. The curing of intractable, biochemically complex diseases requires understanding of the disease basics, but it does not require understanding of the disease details. For wild type capsid II, cryo-EM revealed the complexity of inter-gp10 subunit interactions to be so high that accidental sealing was improbable. Thus, capsids were proposed to be in states selected for function during deoxyribonucleic acid packaging. The hyper-expansion required shell thinning to the point that ß-sheet was proposed as the likely dominant conformation of gp10 major shell protein. The expected increase of a-sheet content for abiotically generated peptides suggests that nests are imprints from times before the existence of living organisms. The idea is that this structure was not completely replaced when increased diversity and chirality arrived for biological amino acids.
