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-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.
Stoll
R
R
Abteilung für Physikalische Biochemie des Physiologisch-chemischen Institutes der Universität Tübingen, FRG.
Voelter
W
W
Holak
T A
TA
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D020005:Propanols; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions; D013947:Thymosin / Q000737:chemistry*; D014867:Water; D006845:Hydrocarbons, Fluorinated
D020005:Propanols; D012996:Solutions; D013947:Thymosin; D014867:Water; C001337:hexafluoroisopropanol; D006845:Hydrocarbons, Fluorinated; C042362:thymosin beta(9)