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Title: Effects of macromolecular crowding on the structure of a protein complex: A small-angle scattering study of superoxide dismutase

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:
 [1];  [2];  [1]
  1. Purdue Univ., West Lafayette, IN (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Spallation Neutron Source (SNS)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
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 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.
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. doi:10.1016/j.bpj.2014.12.046.
Rajapaksha, Ajith, Stanley, Christopher B., and Todd, Brian A. Tue . "Effects of macromolecular crowding on the structure of a protein complex: A small-angle scattering study of superoxide dismutase". United States. doi:10.1016/j.bpj.2014.12.046.
@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 = {2015},
month = {2}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
DOI: 10.1016/j.bpj.2014.12.046

Citation Metrics:
Cited by: 5 works
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