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Conformation of peptide T in aqueous solution. Determination of homonuclear coupling constants by selective HOHAHA techniques
Author(s) -
Zangger Klaus,
Sterk Heinz
Publication year - 1995
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260330603
Subject(s) - homonuclear molecule , chemistry , aqueous solution , coupling constant , peptide , nuclear magnetic resonance spectroscopy , random coil , crystallography , nuclear magnetic resonance , analytical chemistry (journal) , stereochemistry , circular dichroism , organic chemistry , molecule , physics , quantum mechanics , biochemistry
The conformation of Peptide T in aqueous solution was investigated by means of 1 H NMR spectroscopy in one and two dimensions. The data were compared with those obtained previously for the peptide in DMSO solution. While Peptide T forms a β‐turn in DMSO, no evidence was found for such a structure in water. Instead, Peptide T exists in aqueous medium in a random coil conformation with an increased tendency to form a stretched chain at the ends of the peptide backbone. This partly populated β‐strand was identified mostly by the analysis of atomic distances and coupling constants. To evaluate NMR parameters such as chemical shift and scalar coupling constants in the heavily overcrowded spectral regions, selective homonuclear Hartmann‐Hahn transfer was employed, which allows the observation of a distinct multiplet through the excitation of its scalar coupling partner, and subsequent magnetization transfer.