Assignment and conformation of neurotensin in aqueous solution by 1H NMR.
A complete assignment of exchangeable and unexchangeable proton resonances of neurotensin 1-13 in aqueous solution has been carried out with the help of its 1-8 and 8-13 fragments. To detect formation of a secondary structure, the effects of peptide fragmentation, temperature decrease, pH changes and addition of denaturing agents on the neurotensin 1H NMR spectrum were investigated. The small changes observed in all cases support the conclusion that neurotensin exists mainly as a flexible random coiled polypeptidic chain in aqueous solution in agreement with previous CD studies.
D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D009496:Neurotensin / Q000032:analysis*; D009994:Osmolar Concentration; D011487:Protein Conformation; D011489:Protein Denaturation; D011522:Protons; D012996:Solutions; D013696:Temperature; D014508:Urea; D014867:Water
D011522:Protons; D012996:Solutions; D014867:Water; D009496:Neurotensin; D014508:Urea