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

Kristofer Modig; Vibeke W. Jürgensen; Kresten Lindorff-Larsen; Wolfgang Fieber; Henrik G Bohr; Flemming Martin Poulsen

doi:10.1016/j.febslet.2007.09.027

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

Kristofer Modig, Vibeke W. Jürgensen, Kresten Lindorff-Larsen, Wolfgang Fieber, Henrik G Bohr, Flemming Martin Poulsen

Biomolecular Sciences

42 Citations (Scopus)

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.
Udgivelsesdato: 2007-Oct-16

Original language	English
Journal	FEBS Letters
Volume	581
Issue number	25
Pages (from-to)	4965-4971
Number of pages	7
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2007.09.027
Publication status	Published - 2007

Access to Document

10.1016/j.febslet.2007.09.027

Cite this

@article{0f7534b0e9c911dcbee902004c4f4f50,

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

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. Udgivelsesdato: 2007-Oct-16",

author = "Kristofer Modig and J{\"u}rgensen, {Vibeke W.} and Kresten Lindorff-Larsen and Wolfgang Fieber and Bohr, {Henrik G} and Poulsen, {Flemming Martin}",

note = "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",

year = "2007",

doi = "10.1016/j.febslet.2007.09.027",

language = "English",

volume = "581",

pages = "4965--4971",

journal = "F E B S Letters",

issn = "0014-5793",

publisher = "JohnWiley & Sons Ltd",

number = "25",

}

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

SN - 0014-5793

VL - 581

SP - 4965

EP - 4971

JO - F E B S Letters

JF - F E B S Letters

IS - 25

ER -