Reversible Dimerization of Acid-Denatured ACBP Controlled by Helix A4
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Standard
Reversible Dimerization of Acid-Denatured ACBP Controlled by Helix A4. / Fieber, Wolfgang; Kragelund, Birthe Brandt; Meldal, Morten Peter; Poulsen, Flemming M.
I: Biochemistry, Bind 44, Nr. 5, 2005, s. 1375-1384.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Reversible Dimerization of Acid-Denatured ACBP Controlled by Helix A4
AU - Fieber, Wolfgang
AU - Kragelund, Birthe Brandt
AU - Meldal, Morten Peter
AU - Poulsen, Flemming M.
PY - 2005
Y1 - 2005
N2 - The peptide segment corresponding to helix A4 in acyl-coenzyme-A-binding protein (ACBP) is an exceptionally stable helix in the denatured state of the protein as well as in its isolated form. Circular dichroism spectroscopy showed an a-helix content in the helix A4 peptide (HA4) of 45%, and under denaturing conditions at pH 2.3, helix conformations are still populated in 24% of the ensemble of molecules. The structure of HA4 at atomic resolution was assessed using nuclear magnetic resonance (NMR) spectroscopy. Long-range NOEs between remote residues at opposite peptide ends suggested the formation of an antiparallel homodimer, and the resulting structure was treated as the minimum higher-order structure. The dimerization property of helix A4 is maintained in the full-length protein under denaturing conditions. NMR diffusion studies and concentration-dependent experiments on ACBP at low pH proved the formation of dimers and revealed a cooperative stabilization of helix A4 in this process. This emphasizes its special role in the structure formation in the denatured state of ACBP. No dimers are formed in the presence of guanidine hydrochloride, which underlines the fundamental difference between the nature of these two denatured states.
AB - The peptide segment corresponding to helix A4 in acyl-coenzyme-A-binding protein (ACBP) is an exceptionally stable helix in the denatured state of the protein as well as in its isolated form. Circular dichroism spectroscopy showed an a-helix content in the helix A4 peptide (HA4) of 45%, and under denaturing conditions at pH 2.3, helix conformations are still populated in 24% of the ensemble of molecules. The structure of HA4 at atomic resolution was assessed using nuclear magnetic resonance (NMR) spectroscopy. Long-range NOEs between remote residues at opposite peptide ends suggested the formation of an antiparallel homodimer, and the resulting structure was treated as the minimum higher-order structure. The dimerization property of helix A4 is maintained in the full-length protein under denaturing conditions. NMR diffusion studies and concentration-dependent experiments on ACBP at low pH proved the formation of dimers and revealed a cooperative stabilization of helix A4 in this process. This emphasizes its special role in the structure formation in the denatured state of ACBP. No dimers are formed in the presence of guanidine hydrochloride, which underlines the fundamental difference between the nature of these two denatured states.
U2 - 10.1021/bi0481949
DO - 10.1021/bi0481949
M3 - Journal article
C2 - 15683223
VL - 44
SP - 1375
EP - 1384
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 5
ER -
ID: 1094008