TY - JOUR
T1 - Model-independent interpretation of NMR relaxation data for unfolded proteins: the acid-denatured state of ACBP.
AU - Modig, Kristofer
AU - Poulsen, Flemming
N1 - Keywords ACBP - Protein folding - Acid-denaturation - NMR - Relaxation - Model-free
PY - 2008
Y1 - 2008
N2 - We have investigated the acid-unfolded state of acyl-coenzyme A binding protein (ACBP) using (15)N laboratory frame nuclear magnetic resonance (NMR) relaxation experiments at three magnetic field strengths. The data have been analyzed using standard model-free fitting and models involving distribution of correlation times. In particular, a model-independent method of analysis that does not assume any analytical form for the correlation time distribution is proposed. This method explains correlations between model-free parameters and the analytical distribution parameters found by other authors. The analysis also shows that the relaxation data are consistent with and complementary to information obtained from other parameters, especially secondary chemical shifts and residual dipolar couplings, and strengthens the conclusions of previous observations that three out of the four regions that form helices in the native structure appear to contain residual secondary structure also in the acid-denatured state.
AB - We have investigated the acid-unfolded state of acyl-coenzyme A binding protein (ACBP) using (15)N laboratory frame nuclear magnetic resonance (NMR) relaxation experiments at three magnetic field strengths. The data have been analyzed using standard model-free fitting and models involving distribution of correlation times. In particular, a model-independent method of analysis that does not assume any analytical form for the correlation time distribution is proposed. This method explains correlations between model-free parameters and the analytical distribution parameters found by other authors. The analysis also shows that the relaxation data are consistent with and complementary to information obtained from other parameters, especially secondary chemical shifts and residual dipolar couplings, and strengthens the conclusions of previous observations that three out of the four regions that form helices in the native structure appear to contain residual secondary structure also in the acid-denatured state.
U2 - 10.1007/s10858-008-9280-0
DO - 10.1007/s10858-008-9280-0
M3 - Journal article
C2 - 18850278
JO - Journal of Biomolecular N M R
JF - Journal of Biomolecular N M R
SN - 0925-2738
ER -