A hairpin‐loop conformation in tandem repeat sequence of the ice nucleation protein revealed by NMR spectroscopy

FEBS Letters

Ito, Ai²  Tsuda, Sakae²  Matsushima, Norio¹ 

[1] Department of Biophysics, School of Health Sciences, Sapporo Medical University, Sapporo 60,Japan;Bioscience and Chemistry Division, Hokkaido National Industrial Research Institute (HNIRI), Toyohira, Sapporo 62, Japan

关键词: Ice nucleation protein;    Pseudomonas syringae;    Two-dimensional NMR;    Hairpin-loop conformation;    INP24;    a 24-residue peptide of ice-nucleation protein;    NOE;    nuclear Overhauser enhancement;    COSY;    chemical shift correlated spectroscopy;    NOESY;    2D NOE spectroscopy;    ROESY;    2D rotating-frame Overhauser spectroscopy;   

DOI  :  10.1016/S0014-5793(97)00515-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The ¹H-NMR spectrum of a synthetic 24-residue peptide (A¹-G-V-D-S-S-L-I-A-G-Y-G-S-T-Q-T-S-G-S-D-S-A-L-T²⁴; 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 Leu⁷, Ile⁸, Ala⁹, and the ring-protons of Tyr¹¹ was indicated from the observation of the inter-molecular nuclear Overhauser enhancement (NOE) effect. Hydrogen-bonding was strongly suggested for the NH group of Leu⁷ 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, -Leu⁷-Ile⁸-Ala⁹-Gly¹⁰-Tyr¹¹-Gly¹².

【 授权许可】

Unknown