Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences.
- Huan‐Xiang Zhou, G. Rivas, A. Minton
- ChemistryAnnual Review of Biophysics
- 7 May 2008
Theoretical and experimental approaches to the characterization of crowding- and confinement-induced effects in systems approaching the complexity of living organisms are suggested.
The Influence of Macromolecular Crowding and Macromolecular Confinement on Biochemical Reactions in Physiological Media*
- A. Minton
- BiologyJournal of Biological Chemistry
- 6 April 2001
To properly assess the physiological role of a particular reaction or set of reactions characterized in vitro, it is important to consider the possible influence of crowding and/or confinement upon the reaction in its physiological milieu.
Macromolecular crowding: biochemical, biophysical, and physiological consequences.
- S. Zimmerman, A. Minton
- Chemistry, BiologyAnnual Review of Biophysics and Biomolecular…
- 1993
This paper presents a meta-analyses of the macromolecular determinants of reaction rates and volume in a solution and describes the mechanisms leading to these rates and volumes.
Excluded volume as a determinant of macromolecular structure and reactivity
- A. Minton
- Chemistry
- 1 October 1981
The effect of excluded volume on the thermodynamic activity of globular macromolecules and macromolecular complexes in solution is studied in the hard‐particle approximation. Activity coefficients…
Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: macromolecular crowding and protein stability revisited.
- A. Minton
- BiologyBiophysical Journal
- 1 February 2005
Statistical-thermodynamic models for the excluded volume interaction between an unfolded polypeptide chain and a hard sphere or hard rod cosolute are presented, permitting estimation of the free…
Cell biology: Join the crowd
Cells are packed with large molecules. The ramifications of this 'crowding' for a wide range of intracellular processes are only now becoming more generally understood.
The effect of volume occupancy upon the thermodynamic activity of proteins: some biochemical consequences
- A. Minton
- BiologyMolecular and Cellular Biochemistry
- 2004
Experimental studies of the effect of ‘inert’ macromolecules on protein structure and/or function are reviewed, and it is found that under favorable circumstances the simplified models can provide a satisfactory semiquantitative description of the data.
Protein aggregation in crowded environments
The quantitative effects of crowding on protein aggregation and the role of molecular chaperones in combating this problem are discussed.
Effect of dextran on protein stability and conformation attributed to macromolecular crowding.
- K. Sasahara, P. McPhie, A. Minton
- Chemistry, BiologyJournal of Molecular Biology
- 28 February 2003
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