Journal
BIOCHEMISTRY
Volume 57, Issue 11, Pages 1681-1684Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.8b00061
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Funding
- National Science Foundation [MCB-1410854, CHE-1607359]
- National Institutes of Health [NIGMS] [F31 GM126763, T32 GM008570]
- National Cancer Institute [P30 CA016086]
- NATIONAL CANCER INSTITUTE [P30CA016086] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM008570, F31GM126763] Funding Source: NIH RePORTER
- Direct For Biological Sciences [1410854] Funding Source: National Science Foundation
- Direct For Mathematical & Physical Scien [1607359] Funding Source: National Science Foundation
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Protein-protein interactions are fundamental to biology yet are rarely studied under physiologically relevant conditions where the concentration of macromolecules can exceed 300 g/L. These high concentrations cause cosolute-complex contacts that are absent in dilute buffer. Understanding such interactions is important because they organize the cellular interior. We used( 19)F nuclear magnetic resonance, the dimer-forming A34F variant of the model protein GB1, and the cosolutes bovine serum albumin (BSA) and lysozyme to assess the effects of repulsive and attractive charge-charge dimer-cosolute interactions on dimer stability. The interactions were also manipulated via charge-change variants and by changing the pH. Charge-charge repulsions between BSA and GB1 stabilize the dimer, and the effects of lysozyme indicate a role for attractive interactions. The data show that chemical interactions can regulate the strength of protein-protein interactions under physiologically relevant crowded conditions and suggest a mechanism for tuning the equilibrium thermodynamics of protein- protein interactions in cells.
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