title: Picosecond to nanosecond dynamics provide a source of conformational entropy for protein folding.
abstract: Myoglobin can be trapped in fully folded structures, partially folded molten globules, and unfolded states under stable equilibrium conditions. Here, we report an experimental study on the conformational dynamics of different folded conformational states of apo- and holomyoglobin in solution. Global protein diffusion and internal molecular motions were probed by neutron time-of-flight and neutron backscattering spectroscopy on the picosecond and nanosecond time scales. Global protein diffusion was found to depend on the α-helical content of the protein suggesting that charges on the macromolecule increase the short-time diffusion of protein. With regard to the molten globules, a gel-like phase due to protein entanglement and interactions with neighbouring macromolecules was visible due to a reduction of the global diffusion coefficients on the nanosecond time scale. Diffusion coefficients, residence and relaxation times of internal protein dynamics and root mean square displacements of localised internal motions were determined for the investigated structural states. The difference in conformational entropy ΔSconf of the protein between the unfolded and the partially or fully folded conformations was extracted from the measured root mean square displacements. Using thermodynamic parameters from the literature and the experimentally determined ΔSconf values we could identify the entropic contribution of the hydration shell ΔShydr of the different folded states. Our results point out the relevance of conformational entropy of the protein and the hydration shell for stability and folding of myoglobin.
authors.affiliation: Jülich Centre for Neutron Science JCNS and Institute for Complex Systems ICS, Forschungszentrum Jülich GmbH, 52425 Jülich, Germany. a.stadler@fz-juelich.de.
authors.forename: Andreas M
authors.initials: AM
authors.lastname: Stadler
authors.affiliation: ISIS Facility, Rutherford Appleton Laboratory, Didcot OX11 0QX, UK.
authors.forename: Franz
authors.initials: F
authors.lastname: Demmel
authors.affiliation: Institut Laue-Langevin, 71 Avenue des Martyrs, CS 20156, 38042 Grenoble Cedex 9, France.
authors.forename: Jacques
authors.initials: J
authors.lastname: Ollivier
authors.affiliation: Institut Laue-Langevin, 71 Avenue des Martyrs, CS 20156, 38042 Grenoble Cedex 9, France.
authors.forename: Tilo
authors.initials: T
authors.lastname: Seydel
mesh_terms: D019277:Entropy; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding; D013997:Time Factors