Nonnative capping structure initiates helix folding in an annexin I fragment. A 1H NMR conformational study

B OdaertA Sanson


A 21-residue peptide, P1AQFD5ADELR10AAMKG15LGTDE20D, corresponding to the (helix A)-loop motif of the second repeat of human annexin I, was synthesized and studied by 2D proton NMR. The conformational properties of the peptide were characterized at different temperatures in pure aqueous solution and in a TFE/H2O (1:4 v/v) mixture. In pure aqueous solution, the peptide adopts a preferred conformation, comprising both elements of native and nonnative structures. A high alpha helix content is present in the DADELRA segment, which corresponds to an initiation site in the middle of the native alpha helix sequence. At the N-terminus flanking region, a particular nonnative folding is revealed by the J(NH-CH alpha) coupling constants and a set of unusual NOE connectivities which correspond to a helix interrupt at the first D residue. Addition of relatively small amount of TFE restores the native helix fold at the C-terminus but not at the N-terminus. On the contrary, the nonnative N-terminus structure is clearly stabilized by TFE. Our data indicate that this structure comprises (i) an Asp5-x-x-Glu8 N-terminal capping box, as recently named by Harper and Rose [Harper, E. T., & Rose, G. D. (1993) Biochemistry 32, 7605-7609], (ii) a (i,i ...Continue Reading


Mar 26, 1998·Protein Science : a Publication of the Protein Society·R Aurora, G D Rose
Jul 31, 1998·Protein Science : a Publication of the Protein Society·R GueroisA Sanson
May 3, 2013·The Journal of Chemical Physics·Changjun ChenYi Xiao
Oct 28, 2009·Journal of Computational Chemistry·Changjun Chen, Yi Xiao
Jan 23, 1999·The Journal of Biological Chemistry·J GaoH Yan
Oct 4, 2012·Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics·Changjun ChenYi Xiao

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