Effects of Macromolecular Crowding on the Structure of a Protein Complex: A Small-Angle Scattering Study of Superoxide Dismutase

Rajapaksha, Ajith; Stanley, Christopher B.; Todd, Brian A.

doi:10.1016/j.bpj.2014.12.046

Title: Effects of Macromolecular Crowding on the Structure of a Protein Complex: A Small-Angle Scattering Study of Superoxide Dismutase

Full Record
Other Related Research

Abstract

Macromolecular crowding can alter the structure and function of biological macromolecules. We used small angle scattering (SAS) to measure the change in size of a protein complex, superoxide dismutase (SOD), induced by macromolecular crowding. Crowding was induced using 400 MW polyethylene glycol (PEG), triethylene glycol (TEG), methyl- -glucoside ( -MG) and trimethylamine N-oxide (TMAO). Parallel small angle neutron scattering (SANS) and small angle x-ray scattering (SAXS) allowed us to unambiguously attribute apparent changes in radius of gyration to changes in the structure of SOD. For a 40% PEG solution, we find that the volume of SOD was reduced by 9%. Considering the osmotic pressure due to PEG, this deformation corresponds to a highly compressible structure. SAXS done in the presence of TEG suggests that for further deformation beyond a 9% decrease in volume the resistance to deformation may increase dramatically.

Authors:: Rajapaksha, Ajith; Stanley, Christopher B.; Todd, Brian A.

Publication Date:: Sun Feb 01 00:00:00 EST 2015

Research Org.:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)

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

OSTI Identifier:: 1233994

Alternate Identifier(s):: OSTI ID: 1185824

Grant/Contract Number:: AC05-00OR22725

Resource Type:: Published Article

Journal Name:: Biophysical Journal

Additional Journal Information:: Journal Name: Biophysical Journal Journal Volume: 108 Journal Issue: 4; Journal ID: ISSN 0006-3495

Publisher:: Elsevier

Country of Publication:: United States

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES

Citation Formats


                    Rajapaksha, Ajith, Stanley, Christopher B., and Todd, Brian A. Effects of Macromolecular Crowding on the Structure of a Protein Complex: A Small-Angle Scattering Study of Superoxide Dismutase.  United States: N. p., 2015. 
Web.  doi:10.1016/j.bpj.2014.12.046.

Copy to clipboard


                    Rajapaksha, Ajith, Stanley, Christopher B., & Todd, Brian A. Effects of Macromolecular Crowding on the Structure of a Protein Complex: A Small-Angle Scattering Study of Superoxide Dismutase.  United States.  https://doi.org/10.1016/j.bpj.2014.12.046

Copy to clipboard


                    Rajapaksha, Ajith, Stanley, Christopher B., and Todd, Brian A. Sun .  
"Effects of Macromolecular Crowding on the Structure of a Protein Complex: A Small-Angle Scattering Study of Superoxide Dismutase".  United States.  https://doi.org/10.1016/j.bpj.2014.12.046.

Copy to clipboard


                    
@article{osti_1233994,

  title        = {Effects of Macromolecular Crowding on the Structure of a Protein Complex: A Small-Angle Scattering Study of Superoxide Dismutase},

  author       = {Rajapaksha, Ajith and Stanley, Christopher B. and Todd, Brian A.},

  abstractNote = {Macromolecular crowding can alter the structure and function of biological macromolecules. We used small angle scattering (SAS) to measure the change in size of a protein complex, superoxide dismutase (SOD), induced by macromolecular crowding. Crowding was induced using 400 MW polyethylene glycol (PEG), triethylene glycol (TEG), methyl- -glucoside ( -MG) and trimethylamine N-oxide (TMAO). Parallel small angle neutron scattering (SANS) and small angle x-ray scattering (SAXS) allowed us to unambiguously attribute apparent changes in radius of gyration to changes in the structure of SOD. For a 40% PEG solution, we find that the volume of SOD was reduced by 9%. Considering the osmotic pressure due to PEG, this deformation corresponds to a highly compressible structure. SAXS done in the presence of TEG suggests that for further deformation beyond a 9% decrease in volume the resistance to deformation may increase dramatically.},

  doi          = {10.1016/j.bpj.2014.12.046},

  journal      = {Biophysical Journal},

  number       = 4,

  volume       = 108,

  place        = {United States},

  year         = {Sun Feb 01 00:00:00 EST 2015},

  month        = {Sun Feb 01 00:00:00 EST 2015}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
https://doi.org/10.1016/j.bpj.2014.12.046

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 15 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

Macromolecular Crowding Affects Voltage-Dependent Alamethicin Pore Formation in Lipid Bilayer Membranes

Journal Article McClintic, William T. ; Taylor, Graham J. ; Simpson, Michael L. ; ... - Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry

Macromolecular crowding is known to modulate chemical equilibria, reaction rates, and molecular binding events, both in aqueous solutions and at lipid bilayer membranes, natural barriers that enclose the crowded environments of cells and their subcellular compartments. Previous studies on the effects of macromolecular crowding in aqueous compartments on conduction through membranes have focused on single-channel ionic conduction through previously formed pores at thermodynamic equilibrium. Furthermore, the effects of macromolecular crowding on the mechanism of pore formation itself were studied using the droplet interface bilayer (DIB) technique with the voltage-dependent pore-forming peptide alamethicin (alm). Macromolecular crowding was varied using 8 kDamore »« less
Cited by 7
https://doi.org/10.1021/acs.jpcb.0c01650

Full Text Available
Perylene Diimide as a Precise Graphene-like Superoxide Dismutase Mimetic

Journal Article Jalilov, Almaz S. ; Nilewski, Lizanne G. ; Berka, Vladimir ; ... - ACS Nano

Here we show that the active portion of a graphitic nanoparticle can be mimicked by a perylene diimide (PDI) to explain the otherwise elusive biological and electrocatalytic activity of the nanoparticle construct. Development of molecular analogues that mimic the antioxidant properties of oxidized graphenes, in this case the poly(ethylene glycolated) hydrophilic carbon clusters (PEG–HCCs), will afford important insights into the highly efficient activity of PEG–HCCs and their graphitic analogues. PEGylated perylene diimides (PEGn–PDI) serve as well-defined molecular analogues of PEG–HCCs and oxidized graphenes in general, and their antioxidant and superoxide dismutase-like (SOD-like) properties were studied. PEGn–PDIs have two reversible reductionmore »« less
https://doi.org/10.1021/acsnano.6b08211
Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding

Journal Article Banks, Anthony ; Qin, Sanbo ; Weiss, Kevin L. ; ... - Biophysical Journal

Conformational malleability allows intrinsically disordered proteins (IDPs) to respond agilely to their environments, such as nonspecifically interacting with in vivo bystander macromolecules (or crowders). Previous studies have emphasized conformational compaction of IDPs due to steric repulsion by macromolecular crowders, but effects of soft attraction are largely unexplored. Here we studied the conformational ensembles of the IDP FlgM in both polymer and protein crowders by small-angle neutron scattering. As crowder concentrations increased, the mean radius of gyration of FlgM first decreased but then exhibited an uptick. Ensemble optimization modeling indicated that FlgM conformations under protein crowding segregated into two distinct populations,more »« less
Cited by 44
https://doi.org/10.1016/j.bpj.2018.01.011
Molecular Crowding Stabilizes Folded RNA Structure by the Excluded Volume Effect

Journal Article Kilburn, Duncan ; Roh, Joon Ho ; Guo, Liang ; ... - J. Am. Chem. Soc.

Crowder molecules in solution alter the equilibrium between folded and unfolded states of biological macromolecules. It is therefore critical to account for the influence of these other molecules when describing the folding of RNA inside the cell. Small angle X-ray scattering experiments are reported on a 64 kDa bacterial group I ribozyme in the presence of polyethylene-glycol 1000 (PEG-1000), a molecular crowder with an average molecular weight of 1000 Da. In agreement with expected excluded volume effects, PEG favors more compact RNA structures. First, the transition from the unfolded to the folded (more compact) state occurs at lower MgCl{sub 2}more »« less
https://doi.org/10.1021/ja101500g
Inhibition of Microtubule Depolymerization by Osmolytes

Journal Article Bachand, George D. ; Jain, Rishi ; Ko, Randy ; ... - Biomacromolecules

Microtubule dynamics play a critical role in the normal physiology of eukaryotic cells as well as a number of cancers and neurodegenerative disorders. The polymerization/depolymerization of microtubules is regulated by a variety of stabilizing and destabilizing factors, including microtubule-associated proteins and therapeutic agents (e.g., paclitaxel, nocodazole). Here in this paper, we describe the ability of the osmolytes polyethylene glycol (PEG) and trimethylamine-N-oxide (TMAO) to inhibit the depolymerization of individual microtubule filaments for extended periods of time (up to 30 days). We further show that PEG stabilizes microtubules against both temperature- and calcium-induced depolymerization. Our results collectively suggest that the observedmore »« less
Cited by 14
https://doi.org/10.1021/acs.biomac.7b01799

Full Text Available

Similar Records