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FEBS Lett. 2007 Oct 16;581(25):4965-71. Epub 2007 Sep 24.

Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis.

Author information

1
Structural Biology and NMR Laboratory, Department of Molecular Biology, University of Copenhagen, Copenhagen Biocenter, Ole Maaløes Vej 5, DK-2200, Copenhagen, Denmark.

Abstract

A simple alternative method for obtaining "random coil" chemical shifts by intrinsic referencing using the protein's own peptide sequence is presented. These intrinsic random coil backbone shifts were then used to calculate secondary chemical shifts, that provide important information on the residual secondary structure elements in the acid-denatured state of an acyl-coenzyme A binding protein. This method reveals a clear correlation between the carbon secondary chemical shifts and the amide secondary chemical shifts 3-5 residues away in the primary sequence. These findings strongly suggest transient formation of short helix-like segments, and identify unique sequence segments important for protein folding.

PMID:
17910956
DOI:
10.1016/j.febslet.2007.09.027
[Indexed for MEDLINE]
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