1H-NMR of reverse micelles. II: Conformational studies of peptides and proteins in the AOT/water/isooctane system.
The interaction of AOT reverse micelles with Met-enkephalin, the pancreatic secretory trypsin inhibitor (PSTI) and the epidermal growth factor (EGF) is examined by NMR methods and the three systems are compared. While Met-enkephalin adopts a folded conformation, PSTI appears to become highly flexible, suggestive of a non-specific interaction with the micelles. On the other hand, the EGF spectrum shows that, although the main globular features of the protein are retained in the presence of AOT, the C-terminal fragment has to rearrange its conformation when put in contact with the micelle wall.
D004143:Dioctyl Sulfosuccinic Acid; D004744:Enkephalin, Methionine / Q000032:analysis; D004815:Epidermal Growth Factor / Q000032:analysis; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008823:Micelles; D009795:Octanes; D010455:Peptides / Q000032:analysis*; D011487:Protein Conformation; D011522:Protons; D013386:Succinates; D014359:Trypsin Inhibitor, Kazal Pancreatic / Q000032:analysis; D014867:Water
D008823:Micelles; D009795:Octanes; D010455:Peptides; D011522:Protons; D013386:Succinates; D014867:Water; D004143:Dioctyl Sulfosuccinic Acid; D014359:Trypsin Inhibitor, Kazal Pancreatic; D004744:Enkephalin, Methionine; D004815:Epidermal Growth Factor; C045798:2,2,4-trimethylpentane