Conformation of thymosin beta 9 in water/fluoroalcohol solution determined by NMR spectroscopy

Biopolymers. 1997 May;41(6):623-34. doi: 10.1002/(SICI)1097-0282(199705)41:6<623::AID-BIP3>3.0.CO;2-S.


The conformation of thymosin beta 9 in solution of 40% (v/v) 1,1,1,3,3,3-hexafluoro-2-propanol-d2 in water has been investigated by two-dimensional 1H-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 distance constraints derived from nuclear Overhauser enhancement measurements. 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-terminus of thymosin beta 9 shows random-coil structure only.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Propanols
  • Protein Conformation
  • Protein Structure, Secondary
  • Solutions
  • Thymosin / chemistry*
  • Water


  • Propanols
  • Solutions
  • Water
  • hexafluoroisopropanol
  • Thymosin
  • thymosin beta(9)