13C and 13C chemical shifts as a tool to delineate -hairpin structures in peptides

Authors: Santiveri C.M.; Rico M.; Jiménez M.A.

Source: Journal of Biomolecular NMR, Volume 19, Number 4, April 2001 , pp. 331-345(15)

Publisher: Springer

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Abstract:

Unravelling the factors that contribute to the formation and the stability of bgr -sheet structure in peptides is a subject of great current interest. A bgr -hairpin, the smallest bgr -sheet motif, consists of two antiparallel hydrogen-bonded bgr -strands linked by a loop region. We have performed a statistical analysis on protein bgr -hairpins showing that the most abundant types of bgr -hairpins, 2:2, 3:5 and 4:4, have characteristic patterns of ^13C_&agr; and ^13C_&bgr; conformational shifts, as expected on the basis of their phgr and psgr angles. This fact strongly supports the potential value of ^13C_&agr; and ^13C_&bgr; conformational shifts as a means to identify bgr -hairpin motifs in peptides. Their usefulness was confirmed by analysing the patterns of ^13C_&agr; and ^13C_&bgr; conformational shifts in 13 short peptides, 10–15 residues long, that adopt bgr -hairpin structures in aqueous solution. Furthermore, we have investigated their potential as a method to quantify bgr -hairpin populations in peptides.