TY - JOUR
T1 - Formation of Native and Non-native Interactions in Ensembles of Denatured ACBP Molecules from Paramagnetic Relaxation Enhancement Studies
AU - Kristjansdottir, S.
AU - Lindorff-Larsen, Kresten
AU - Fieber, W.
AU - Dobson, Christopher M.
AU - Vendruscolo, Michele
AU - Poulsen, Flemming M.
PY - 2005
Y1 - 2005
N2 - Paramagnetic relaxation enhancement measurements in the denatured state of ACBP have provided distance restraints that have been used in computer simulations to determine the conformational ensembles representing the denatured states of ACBP under a variety of conditions. A detailed comparison of the residual structure in the denatured state of ACBP under these different conditions has enabled us to infer that regions in the N and C-terminal parts of the protein sequence have a high tendency to interact in the unfolded state under physiological conditions. By comparing the structural features in the denatured states with those in the transition state for folding we also provided new insights into the mechanism of formation of the native state of this protein.Keywords: protein folding; denatured state; NMR; molecular dynamics; structural studiesAbbreviations: ACBP, acyl coenzyme A binding protein; GuHCl, guanidinium chloride; HSQC, heteronuclear single quantum coherence; MTSL, (1-oxyl-2,2,5,5-tetrametyl-3-pyrroline-3-methyl)methane sulfonate; PRE, paramagnetic relaxation enhancement
AB - Paramagnetic relaxation enhancement measurements in the denatured state of ACBP have provided distance restraints that have been used in computer simulations to determine the conformational ensembles representing the denatured states of ACBP under a variety of conditions. A detailed comparison of the residual structure in the denatured state of ACBP under these different conditions has enabled us to infer that regions in the N and C-terminal parts of the protein sequence have a high tendency to interact in the unfolded state under physiological conditions. By comparing the structural features in the denatured states with those in the transition state for folding we also provided new insights into the mechanism of formation of the native state of this protein.Keywords: protein folding; denatured state; NMR; molecular dynamics; structural studiesAbbreviations: ACBP, acyl coenzyme A binding protein; GuHCl, guanidinium chloride; HSQC, heteronuclear single quantum coherence; MTSL, (1-oxyl-2,2,5,5-tetrametyl-3-pyrroline-3-methyl)methane sulfonate; PRE, paramagnetic relaxation enhancement
U2 - 10.1016/j.jmb.2005.01.009
DO - 10.1016/j.jmb.2005.01.009
M3 - Journal article
SN - 0022-2836
VL - 347
SP - 1053
EP - 1062
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 5
ER -