Reduced Internal Friction by Osmolyte Interaction in Intrinsically Disordered Myelin Basic Protein

Stingaciu, Laura R.; Biehl, Ralf; Changwoo, Do; Richter, Dieter; Stadler, Andreas M.

doi:10.1021/acs.jpclett.9b03001

Title: Reduced Internal Friction by Osmolyte Interaction in Intrinsically Disordered Myelin Basic Protein

Journal Article · 15 December 2019 · Journal of Physical Chemistry Letters

DOI: https://doi.org/10.1021/acs.jpclett.9b03001 · OSTI ID:1869125

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Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS) outstation Juelich Centre for Neutron Science (JCNS), Forschungszentrum Juelich GmbH
Juelich Research Centre (Germany). Juelich Centre for Neutron Science (JCNS)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS) outstation Juelich Centre for Neutron Science (JCNS), Forschungszentrum Juelich GmbH; RWTH Aachen Univ. (Germany). Institute of Physical Chemistry

Urea is a strong denaturing osmolyte that disrupts noncovalent bonds in proteins. Here, we present a small-angle neutron scattering (SANS) and neutron spin–echo spectroscopy (NSE) study on the structure and dynamics of the intrinsically disordered myelin basic protein (MBP) denatured by urea. SANS results show that urea-denatured MBP is more compact than ideal polymers, while its secondary structure content is entirely lost. Additionally, NSE experiments reveal concomitantly an increase of the relaxation time and of the amplitude of internal motions in urea-denatured MBP as compared to native MBP. If interpreted in terms of the Zimm model including internal friction (ZIF), the internal friction parameter decreased by a factor of 6.5. Urea seems to not only smooth local energy barriers, reducing internal friction on a local scale, but also significantly reduces the overall depth of the global energy landscape. This leads to a nearly complete loss of restoring forces beyond entropic forces and in turn allows for larger motional amplitudes. Obviously, the noncovalent H-bonds are largely eliminated, driving the unfolded protein to be more similar to a synthetic polymer.

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Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1869125

Journal Information:: Journal of Physical Chemistry Letters, Journal Name: Journal of Physical Chemistry Letters Journal Issue: 1 Vol. 11; ISSN 1948-7185

Publisher:: American Chemical SocietyCopyright Statement

Country of Publication:: United States

Language:: English

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37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
chemical structure
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