Premium
Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis
Author(s) -
Modig Kristofer,
Jürgensen Vibeke W.,
Lindorff-Larsen Kresten,
Fieber Wolfgang,
Bohr Henrik G.,
Poulsen Flemming M.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.09.027
Subject(s) - random coil , chemical shift , protein secondary structure , chemistry , protein folding , folding (dsp implementation) , sequence (biology) , helix bundle , helix (gastropod) , crystallography , peptide sequence , protein structure , biophysics , biochemistry , biology , ecology , snail , gene , electrical engineering , engineering
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.