Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study

Journal article


Publication Details

Author(s): Gaspar AM, Appavou MS, Busch S, Unruh T, Doster W
Journal: European Biophysics Journal With Biophysics Letters
Publisher: SPRINGER
Publication year: 2008
Volume: 37
Journal issue: 5
Pages range: 573-582
ISSN: 0175-7571


Abstract


Casein proteins belong to the class of natively disordered proteins. The existence of disordered biologically active proteins questions the assumption that a well-folded structure is required for function. A hypothesis generally put forward is that the unstructured nature of these proteins results from the functional need of a higher flexibility. This interplay between structure and dynamics was investigated in a series of time-of-flight neutron scattering experiments, performed on casein proteins, as well as on three well-folded proteins with distinct secondary structures, namely, myoglobin (alpha), lysozyme (alpha/beta) and concanavalin A (beta). To illustrate the subtraction of the solvent contribution from the scattering spectra, we used the dynamic susceptibility spectra emphasizing the high frequency part of the spectrum, where the solvent dominates. The quality of the procedure is checked by comparing the corrected spectra to those of the dry and hydrated protein with negligible solvent contamination. Results of spectra analysis reveal differences in motional amplitudes of well-folded proteins, where beta-sheet structures appear to be more rigid than a cluster of alpha-helices. The disordered caseins display the largest conformational displacements. Moreover their global diffusion rates deviate from the expected dependence, suggesting further large-scale conformational motions.



FAU Authors / FAU Editors

Unruh, Tobias Prof. Dr.
Professur für Nanomaterialcharakterisierung (Streumethoden)


External institutions
Forschungszentrum Jülich GmbH (FZJ)
Technische Universität München (TUM)


How to cite

APA:
Gaspar, A.M., Appavou, M.-S., Busch, S., Unruh, T., & Doster, W. (2008). Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study. European Biophysics Journal With Biophysics Letters, 37(5), 573-582. https://dx.doi.org/10.1007/s00249-008-0266-3

MLA:
Gaspar, A. M., et al. "Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study." European Biophysics Journal With Biophysics Letters 37.5 (2008): 573-582.

BibTeX: 

Last updated on 2018-10-08 at 15:38