Folding propensity of intrinsically disordered proteins by osmotic stress

Mansouri, Amanda L.; Grese, Laura N.; Rowe, Erica L.; Pino, James C.; Chennubhotla, S. Chakra; Ramanathan, Arvind; O'Neill, Hugh Michael; Berthelier, Valerie; Stanley, Christopher B.

doi:10.1039/C6MB00512H

Title: Folding propensity of intrinsically disordered proteins by osmotic stress

Journal Article · Tue Oct 11 00:00:00 EDT 2016 · Molecular BioSystems

DOI:https://doi.org/10.1039/C6MB00512H· OSTI ID:1333084

Mansouri, Amanda L. ^[1]; Grese, Laura N. ^[2]; Rowe, Erica L. ^[2]; Pino, James C. ^[3]; Chennubhotla, S. Chakra ^[4]; Ramanathan, Arvind ^[3]; O'Neill, Hugh Michael ^[3]; Berthelier, Valerie ^[1]; Stanley, Christopher B. ^[3]

Univ. of Tennessee, Knoxville, TN (United States)
Univ. of Tennessee, Knoxville, TN (United States); Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Univ. of Pittsburgh, Pittsburgh, PA (United States)

Proteins imparted with intrinsic disorder conduct a range of essential cellular functions. To better understand the folding and hydration properties of intrinsically disordered proteins (IDPs), we used osmotic stress to induce conformational changes in nuclear co-activator binding domain (NCBD) and activator for thyroid hormone and retinoid receptor (ACTR). Osmotic stress was applied by the addition of small and polymeric osmolytes, where we discovered that water contributions to NCBD folding always exceeded those for ACTR. Both NCBD and ACTR were found to gain a-helical structure with increasing osmotic stress, consistent with their folding upon NCBD/ACTR complex formation. Using small-angle neutron scattering (SANS), we further characterized NCBD structural changes with the osmolyte ethylene glycol. Here a large reduction in overall size initially occurred before substantial secondary structural change. In conclusion, by focusing on folding propensity, and linked hydration changes, we uncover new insights that may be important for how IDP folding contributes to binding.

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

Sponsoring Organization:: USDOE Laboratory Directed Research and Development (LDRD) Program

Grant/Contract Number:: AC05-00OR22725

OSTI ID:: 1333084

Journal Information:: Molecular BioSystems, Vol. 12, Issue 12; ISSN 1742-206X

Publisher:: Royal Society of ChemistryCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 11 works

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