CONFORMATION OF THYMOSIN BETA(9) IN WATER FLUOROALCOHOL SOLUTION DETERMINED BY NMR-SPECTROSCOPY/

The conformation of thymosin beta(9) in solution of 40% (v/v) 1,1,1,3, 3, 3-hexafluoro-2-propanol-d(2) in water has been investigated by two -dimensional H-1-nmr spectroscopy. Under this condition thymosin beta( 9) adopts an ordered structure. The determination of the conformation of the peptide was based on a set of 304 approximate interproton dista nce constraints derived from nuclear Overhauser enhancement measuremen ts. The conformation of thymosin beta(9) includes two helical regions from residues 4 to 27 and 32 to 41. The two helices are separated by a poorly defined loop region between amino acids 28 and 31; the N-termi nus of thymosin beta(9) shows random-coil structure only. (C) 1997 Joh n Wiley & Sons, Inc.