Detection of initiation sites in protein folding of the four helix bundle ACBP by chemical shift analysis.
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.
Modig
Kristofer
K
Structural Biology and NMR Laboratory, Department of Molecular Biology, University of Copenhagen, Copenhagen Biocenter, Ole Maaløes Vej 5, DK-2200, Copenhagen, Denmark.
Jürgensen
Vibeke W
VW
Lindorff-Larsen
Kresten
K
Fieber
Wolfgang
W
Bohr
Henrik G
HG
Poulsen
Flemming M
FM
D000214:Acyl Coenzyme A / Q000378:metabolism; D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D016415:Sequence Alignment
D000214:Acyl Coenzyme A; D002352:Carrier Proteins