Transient Structures, Ensembles of Structures and Transition States in the Protein Folding Process of a Four Helix Bundle – ACBP
Flemming Poulsen

Transient Structures, Ensembles of Structures and Transition States in the Protein Folding Process of a Four Helix Bundle – ACBP


W.Fieber1, S. Kristjansdottir1, K. Lindorff-Larsen1, 2, K. Teilum1, J. K. Thomsen1, B.B. Kragelund1, M. Vendruscolo2, C.M. Dobson2 and F.M. Poulsen1



1SBiN- Lab, Institute of Molecular Biology, University of Copenhagen, Øster Farimagsgade 2A, DK-1353 Copenhagen, Denmark


2University of Cambridge, University Chemical Laboratory, Lens.eld
Road, Cambridge, CB2 1EW, United Kingdom



NMR spectroscopy has been used to characterize the unfolded states of the four helix bundle protein ACBP at two different unfolding conditions, at low pH and in the presence of the denaturant guanidine hydrochloride. The analysis includes the results obtained by chemical shift, residual dipolar coupling, relaxation and paramagnetic relaxation enhancement in combination with mutation studies. The information about long and short range interactions obtained by these methods will provide the basis for a characterization of the formation of native and non-native like structures preceding the formation of the folding transition state at the two different folding and unfolding conditions.
Recent publications
Formation of Native and Non-native Interactions in Ensembles of Denatured ACBP Molecules from Paramagnetic Relaxation Enhancement Studies
S. Kristjansdottir, K. Lindorff-Larsen, W. Fieber, C. M. Dobson, M. Vendruscolo, and F. M. Poulsen
Journal of Molecular Biology, 347, 1053-1062 (2005)

Determination of an Ensemble of Structures Representing the Denatured State of the Bovine Acyl-Coenzyme A Binding Protein
K. Lindorff-Larsen, S. Kristjansdottir, K. Teilum, W. Fieber, C. M. Dobson, F. M. Poulsen, and M. Vendruscolo.
Journal of the American Chemical Society, 126, 3291-3299 (2004)

Short-range, Long-range and Transition State Interactions in the Denatured State of ACBP from Residual Dipolar Couplings
W.Fieber, S. Kristjansdottir and F. M. Poulsen,
Journal of Molecular Biology 339, 1191-1199 (2004)

Transient intermediary states with high and low folding probabilities in the apparent two-state folding equilibrium of ACBP at low pH.
J K. Thomsen, B. B. Kragelund, K. Teilum, J. Knudsen, and F. M. Poulsen
Journal of Molecular Biology 318, 805-814 (2002)

Early kinetic intermediate in the folding of acyl-coenzyme A binding protein detected by fluorescence labelling and rapid mixing.
K. Teilum, K. Maki, B.B. Kragelund, F. M. Poulsen and H. Roder
Proceedings of the National Academy of Sciences. USA, 99, 9807-9812 (2002)

Transient structure formation in unfolded acyl coenzyme A binding protein observed by site directed spin labelling.
K. Teilum, B. B. Kragelund and F. M. Poulsen
Journal of Molecular Biology 324, 349-357 (2002)