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

Gaspar AM, Appavou MS, Busch S, Unruh T, Doster W (2008)

Publication Status: Published

Publication Type: Journal article

Publication year: 2008

Journal

European Biophysics Journal Springer

Publisher: SPRINGER

Book Volume: 37

Pages Range: 573-582

Journal Issue: 5

DOI: 10.1007/s00249-008-0266-3

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.

Authors with CRIS profile

Tobias Unruh Professur für Nanomaterialcharakterisierung (Streumethoden)

Involved external institutions

Technische Universität München (TUM) DE Germany (DE) Forschungszentrum Jülich / Research Centre Jülich (FZJ) DE Germany (DE)

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, 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 37.5 (2008): 573-582.

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