Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis.
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Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis. / Modig, Kristofer; Jürgensen, Vibeke W.; Lindorff-Larsen, Kresten; Fieber, Wolfgang; Bohr, Henrik G; Poulsen, Flemming Martin.
In: FEBS Letters, Vol. 581, No. 25, 2007, p. 4965-4971.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis.
AU - Modig, Kristofer
AU - Jürgensen, Vibeke W.
AU - Lindorff-Larsen, Kresten
AU - Fieber, Wolfgang
AU - Bohr, Henrik G
AU - Poulsen, Flemming Martin
N1 - Keywords: Acyl Coenzyme A; Amino Acid Sequence; Carrier Proteins; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Sequence Alignment
PY - 2007
Y1 - 2007
N2 - 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. Udgivelsesdato: 2007-Oct-16
AB - 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. Udgivelsesdato: 2007-Oct-16
U2 - 10.1016/j.febslet.2007.09.027
DO - 10.1016/j.febslet.2007.09.027
M3 - Journal article
C2 - 17910956
VL - 581
SP - 4965
EP - 4971
JO - F E B S Letters
JF - F E B S Letters
SN - 0014-5793
IS - 25
ER -
ID: 2998162