DNA compaction in a crowded environment with negatively charged proteins.
We studied the conformational properties of DNA in a salt solution of the strongly charged protein bovine serum albumin. DNA is compacted when a suitable amount of bovine serum albumin is added to the solution due to a crowding effect and strong electrostatic repulsion between DNA and bovine serum albumin, both of which carry negative charges. However, DNA undergoes an unfolding transition with an increase in the salt concentration. This observation contradicts the current understanding of polymer- and salt-induced condensation, ψ condensation. We propose a simple theoretical model by taking into account the competition between the translational entropy of ions and electrostatic interaction.
Krotova
M K
MK
Physics Department, M. V. Lomonosov Moscow State University, Moscow 119992, Russia.
Vasilevskaya
V V
VV
Makita
N
N
Yoshikawa
K
K
Khokhlov
A R
AR
D004247:DNA / Q000737:chemistry*; D019277:Entropy; D007477:Ions; D008856:Microscopy, Fluorescence; D008956:Models, Chemical; D058767:Protein Unfolding / Q000187:drug effects; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D012965:Sodium Chloride / Q000737:chemistry* / Q000494:pharmacology; D012996:Solutions / Q000737:chemistry
D007477:Ions; D012996:Solutions; D012710:Serum Albumin, Bovine; D012965:Sodium Chloride; D004247:DNA