Format

Send to

Choose Destination
See comment in PubMed Commons below
Biopolymers. 1997 May;41(6):623-34.

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

Author information

1
Abteilung für Physikalische Biochemie des Physiologisch-chemischen Institutes der Universität Tübingen, FRG.

Abstract

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.

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Wiley
    Loading ...
    Support Center