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)
Unravelling the factors that contribute to the formation and the stability of -sheet structure in peptides is a subject of great current interest. A -hairpin, the smallest -sheet motif, consists of two antiparallel hydrogen-bonded -strands linked by a loop region. We have performed a statistical analysis on protein -hairpins showing that the most abundant types of -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 and angles. This fact strongly supports the potential value of ^13C_&agr; and ^13C_&bgr; conformational shifts as a means to identify -hairpin motifs in peptides. Their usefulness was confirmed by analysing the patterns of ^13C_&agr; and ^13C_&bgr; conformational shifts in 13 short peptides, 1015 residues long, that adopt -hairpin structures in aqueous solution. Furthermore, we have investigated their potential as a method to quantify -hairpin populations in peptides.
Document Type: Regular paper
Publication date: 2001-04-01