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

K. Modig, Vibeke Würtz Jürgensen, K. Lindorff-Larsen, W. Fieber, Henrik Bohr, F.M. Poulsen

Research output: Contribution to journalJournal articleResearchpeer-review

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 acylcoenzyme 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.
Original languageEnglish
JournalFEBS Letters
Volume581
Issue number25
Pages (from-to)4965-4971
ISSN0014-5793
DOIs
Publication statusPublished - 2007

Keywords

  • residual dipolar coupling
  • protein folding
  • chemical shift
  • NMR
  • unfolded states
  • intrinsic
  • random coil chemical shifts

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