Reduced Internal Friction by Osmolyte Interaction in Intrinsically Disordered Myelin Basic Protein
| Autor: | Laura Stingaciu, Dieter Richter, Do Changwoo, Ralf Biehl, Andreas M. Stadler |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
inorganic chemicals
Models Molecular Protein Denaturation Friction Protein Conformation Astrophysics::High Energy Astrophysical Phenomena Nuclear Theory Neutron scattering 010402 general chemistry 01 natural sciences chemistry.chemical_compound 0103 physical sciences Scattering Small Angle Non-covalent interactions Urea General Materials Science Neutron ddc:530 Physical and Theoretical Chemistry Nuclear Experiment Spectroscopy chemistry.chemical_classification Physics::Biological Physics Quantitative Biology::Biomolecules integumentary system 010304 chemical physics biology technology industry and agriculture Myelin Basic Protein Internal friction 0104 chemical sciences Myelin basic protein Neutron Diffraction chemistry Osmolyte biological sciences Biophysics biology.protein lipids (amino acids peptides and proteins) Software |
| Zdroj: | The journal of physical chemistry letters 11(1), 292-296 (2020). doi:10.1021/acs.jpclett.9b03001 |
| DOI: | 10.1021/acs.jpclett.9b03001 |
| Popis: | 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. 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. |
| Databáze: | OpenAIRE |
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