Journal
PHYSICAL REVIEW LETTERS
Volume 114, Issue 6, Pages -Publisher
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.114.068303
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Funding
- National Science Foundation [CHE 13-61946]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1361946] Funding Source: National Science Foundation
- National Research Foundation of Korea [CG035002] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Experiments show that macromolecular crowding modestly reduces the size of intrinsically disordered proteins even at a volume fraction (phi) similar to that in the cytosol, whereas DNA undergoes a coil-to-globule transition at very small phi. We show using a combination of scaling arguments and simulations that the polymer size (R) over bar (g)(phi) depends on x = (R) over bar (g)(0)/D, where D is the phi-dependent distance between the crowders. If x <= O(1), there is only a small decrease in (R) over bar (g)(phi) as phi increases. When x >> O(1), a cooperative coil-to-globule transition is induced. Our theory quantitatively explains a number of experiments.
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