Table 3.
Folding of the monomers and oligomerization properties of peptides 3a–3n.
Peptide | Folding of the monomer | Oligomerization properties |
---|---|---|
3a | partial | tetramera |
3b | partial | tetramerb |
3c | partial | tetramerb |
3d | partial | tetramerb |
3e | partial | tetramerb |
3f | good | tetramer (with a K1,4 higher than 3a)c |
3g | good | tetramer (with a K1,4 higher than 3a)d |
3h | partial | tetramer (with a K1,4 lower than 3a)e |
3i | partial | ____f |
3j | partial | hexamer or octamerg |
3k | partial | hexamer or octamerg |
3l | partial | ____f |
3m | partial | ____f |
3n | partial | ____f |
The oligomerization state was determined by PFG NMR diffusion measurements and AUC experiments.
The oligomerization state was inferred from similar oligomerization behavior as peptide 3a in concentration-dependent 1H NMR studies.
The oligomerization state was determined by PFG NMR diffusion measurements 46 and 1H NMR concentration studies.
The oligomerization state was inferred from similar oligomerization behavior as peptide 3f in concentration-dependent 1H NMR studies.
The oligomerization state was determined by PFG NMR diffusion measurements 47 and 1H NMR concentration studies.
Some self-association without distinct oligomer formation was observed by concentration-dependant 1H NMR studies.
The oligomerization state was determined by PFG NMR diffusion measurements.48