title: Macromolecular crowding: Macromolecules friend or foe.
abstract: BACKGROUND
  Cellular interior is known to be densely crowded due to the presence of soluble and insoluble macromolecules, which altogether occupy ~40% of the total cellular volume. This results in altered biological properties of macromolecules.
  
  
  METHODS
  Macromolecular crowding is observed to have both positive and negative effects on protein folding, structure, stability and function. Significant data has been accumulated so far on both the aspects. However, most of the review articles so far have focused on the positive aspect of macromolecular crowding and not much attention has been paid on the deleterious aspect of crowding on macromolecules. In order to have a complete knowledge of the effect of macromolecular crowding on proteins and enzymes, it is important to look into both the aspects of crowding to determine its precise role under physiological conditions. To fill the gap in the understanding of the effect of macromolecular crowding on proteins and enzymes, this review article focuses on the deleterious influence of crowding on macromolecules.
  
  
  CONCLUSIONS
  Macromolecular crowding is not always good but also has several deleterious effects on various macromolecular properties. Taken together, the properties of biological macromolecules in vivo appears to be finely regulated by the nature and level of the intracellular crowdedness in order to perform their biological functions appropriately.
  
  
  CONCLUSIONS
  The information provided here gives an understanding of the role played by the nature and level of cellular crowdedness in intensifying and/or alleviating the burden of various proteopathies.
authors.affiliation: Dr. B. R. Ambedkar Centre for Biomedical Research, University of Delhi, Delhi - 110 007, India. Electronic address: shrutimittal4@gmail.com.
authors.forename: Shruti
authors.initials: S
authors.lastname: Mittal
authors.affiliation: Dr. B. R. Ambedkar Centre for Biomedical Research, University of Delhi, Delhi - 110 007, India. Electronic address: rimpy_1989@yahoo.co.in.
authors.forename: Rimpy Kaur
authors.initials: RK
authors.lastname: Chowhan
authors.affiliation: Dr. B. R. Ambedkar Centre for Biomedical Research, University of Delhi, Delhi - 110 007, India. Electronic address: lrsingh@acbr.du.ac.in.
authors.forename: Laishram Rajendrakumar
authors.initials: LR
authors.lastname: Singh
mesh_terms: D030342:Genetic Diseases, Inborn / Q000209:etiology; D046911:Macromolecular Substances / Q000737:chemistry*; D019636:Neurodegenerative Diseases / Q000209:etiology; D066329:Protein Aggregates; D011487:Protein Conformation; D017510:Protein Folding; D055550:Protein Stability; D014783:Viscosity
chemical_list: D046911:Macromolecular Substances; D066329:Protein Aggregates
keywords: Enzyme activity; Excluded volume effect; Protein aggregation; Protein folding; Protein stability