Premium
A hairpin‐loop conformation in tandem repeat sequence of the ice nucleation protein revealed by NMR spectroscopy
Author(s) -
Tsuda Sakae,
Ito Ai,
Matsushima Norio
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00515-2
Subject(s) - chemistry , nuclear magnetic resonance spectroscopy , residue (chemistry) , nuclear overhauser effect , crystallography , hydrogen bond , two dimensional nuclear magnetic resonance spectroscopy , spectroscopy , stereochemistry , chemical shift , molecule , biochemistry , organic chemistry , physics , quantum mechanics
The 1 H‐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 .