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Int. J. Mol. Sci. 2014, 15(12), 23090-23140;

What Macromolecular Crowding Can Do to a Protein

Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., St. Petersburg 194064, Russia
Department of Biophysics, St. Petersburg State Polytechnical University, 29 Polytechnicheskaya St., St. Petersburg 195251, Russia
Department of Molecular Medicine and USF Health Byrd Alzheimerʼs Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd. MDC07, Tampa, FL 33620, USA
Institute for Biological Instrumentation, Russian Academy of Sciences, 4 Institutskaya St., Pushchino, Moscow 142290, Russia
Biology Department, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia
Author to whom correspondence should be addressed.
Received: 31 October 2014 / Revised: 4 December 2014 / Accepted: 5 December 2014 / Published: 12 December 2014
(This article belongs to the Collection Feature Annual Reviews in Molecular Sciences)
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The intracellular environment represents an extremely crowded milieu, with a limited amount of free water and an almost complete lack of unoccupied space. Obviously, slightly salted aqueous solutions containing low concentrations of a biomolecule of interest are too simplistic to mimic the “real life” situation, where the biomolecule of interest scrambles and wades through the tightly packed crowd. In laboratory practice, such macromolecular crowding is typically mimicked by concentrated solutions of various polymers that serve as model “crowding agents”. Studies under these conditions revealed that macromolecular crowding might affect protein structure, folding, shape, conformational stability, binding of small molecules, enzymatic activity, protein-protein interactions, protein-nucleic acid interactions, and pathological aggregation. The goal of this review is to systematically analyze currently available experimental data on the variety of effects of macromolecular crowding on a protein molecule. The review covers more than 320 papers and therefore represents one of the most comprehensive compendia of the current knowledge in this exciting area. View Full-Text
Keywords: macromolecular crowding; excluded volume; protein structure; protein folding; protein function; protein-protein interaction; intrinsically disordered protein; protein aggregation macromolecular crowding; excluded volume; protein structure; protein folding; protein function; protein-protein interaction; intrinsically disordered protein; protein aggregation

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Kuznetsova, I.M.; Turoverov, K.K.; Uversky, V.N. What Macromolecular Crowding Can Do to a Protein. Int. J. Mol. Sci. 2014, 15, 23090-23140.

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