Abstract
An equimolar mixture of avion pancreatic polypeptide (aPP) fragments aPP(1-11)-NH2 and Ac-aPP(12-36) had an electronic circular dichroism (ECD) spectrum that was similar to that of whole aPP in H2O and even more so in 30% (v/v) trifluoroethanol (TFE) in 15 mM Na2HPO 4, but was different from the sum of the spectra of the individual fragments. The vibrational circular dichroism (VCD) spectrum of the combined fragments in 30% (v/v) TFE in 15 mM Na2HPO4 in D 2O was also similar to that of the intact aPP and unlike the sum of the VCD spectra of the fragments. The interaction of these fragments is thus sufficient to support the conformation of whole aPP. This study demonstrates that VCD, in combination with ECD, is useful for the study of protein-protein interactions.
| Original language | English |
|---|---|
| Pages (from-to) | 32-38 |
| Number of pages | 7 |
| Journal | Biopolymers |
| Volume | 83 |
| Issue number | 1 |
| DOIs | |
| State | Published - Sep 2006 |
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All Science Journal Classification (ASJC) codes
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biophysics
Cite this
Avian pancreatic polypeptide fragments refold to native aPP conformation when combined in solution : A CD and VCD study. / Copps, Jeffrey; Murphy, Richard F.; Lovas, Sándor.
In: Biopolymers, Vol. 83, No. 1, 09.2006, p. 32-38.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Avian pancreatic polypeptide fragments refold to native aPP conformation when combined in solution
T2 - A CD and VCD study
AU - Copps, Jeffrey
AU - Murphy, Richard F.
AU - Lovas, Sándor
PY - 2006/9
Y1 - 2006/9
N2 - An equimolar mixture of avion pancreatic polypeptide (aPP) fragments aPP(1-11)-NH2 and Ac-aPP(12-36) had an electronic circular dichroism (ECD) spectrum that was similar to that of whole aPP in H2O and even more so in 30% (v/v) trifluoroethanol (TFE) in 15 mM Na2HPO 4, but was different from the sum of the spectra of the individual fragments. The vibrational circular dichroism (VCD) spectrum of the combined fragments in 30% (v/v) TFE in 15 mM Na2HPO4 in D 2O was also similar to that of the intact aPP and unlike the sum of the VCD spectra of the fragments. The interaction of these fragments is thus sufficient to support the conformation of whole aPP. This study demonstrates that VCD, in combination with ECD, is useful for the study of protein-protein interactions.
AB - An equimolar mixture of avion pancreatic polypeptide (aPP) fragments aPP(1-11)-NH2 and Ac-aPP(12-36) had an electronic circular dichroism (ECD) spectrum that was similar to that of whole aPP in H2O and even more so in 30% (v/v) trifluoroethanol (TFE) in 15 mM Na2HPO 4, but was different from the sum of the spectra of the individual fragments. The vibrational circular dichroism (VCD) spectrum of the combined fragments in 30% (v/v) TFE in 15 mM Na2HPO4 in D 2O was also similar to that of the intact aPP and unlike the sum of the VCD spectra of the fragments. The interaction of these fragments is thus sufficient to support the conformation of whole aPP. This study demonstrates that VCD, in combination with ECD, is useful for the study of protein-protein interactions.
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U2 - 10.1002/bip.20524
DO - 10.1002/bip.20524
M3 - Article
VL - 83
SP - 32
EP - 38
JO - Biopolymers
JF - Biopolymers
SN - 0006-3525
IS - 1
ER -