Abstract
The 1H-NMR spectrum of a synthetic 24-residue peptide (A 1-G-V-D-S-S-L-I-A-G-Y-G-S-T-Q-T-S-G-S-D-S-A-L-T 24; INP24), comprising three repeats of the 8-residue consensus sequence of Pseudomonas syringae ice nucleation protein, was fully assigned using 2-dimensional (2D) NMR spectroscopy at 4°C and 30°C. Close proximity of the aliphatic protons between Leu 7, Ile 8, Ala 9, and the ring-protons of Tyr 11 was indicated from the observation of the inter-molecular nuclear Overhauser enhancement (NOE) effect. Hydrogen-bonding was strongly suggested for the NH group of Leu 7 from its extremely low-temperature coefficient estimated from the temperature dependence of the chemical shift. These results indicate the formation of a hairpin-loop conformation constructed by a hexapeptide segment of INP24, -Leu 7-Ile 8-Ala 9-Gly 10-Tyr 11-Gly 12.
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