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Table 1.

Predicted and observed effects of macromolecular crowding by high concentrations of inert macromolecules

Predicted effect Relevant observations§
Enhancement of equilibrium association of dilute macromolecules (Minton, 1981; Nichol et al., 1981).   Large enhancement in the extent of sickle hemoglobin polymerization (Bookchin et al., 1999); large increase in affinity of DNA-binding proteins for DNA (Zimmerman and Harrison, 1987; Jarvis et al., 1990); enhanced self-association of spectrin (Lindner and Ralston, 1995), actin (Lindner and Ralston, 1997), fibrinogen (Rivas et al., 1999), tubulin (Rivas et al., 1999) and FtsZ (Rivas et al., 2001).  
Acceleration of slow (transition state limited) protein associations (Minton, 1983; Minton, 2001a).   Large increases in the rate of fiber formation by sickle cell hemoglobin (Rotter et al., 2005), actin (Drenckhahn and Pollard, 1986), tubulin (Herzog and Weber, 1978) and fibrin (Wilf et al., 1985). Large increases in the rate of amyloid formation by apoCII (Hatters et al., 2002) and α-synuclein (Shtilerman et al., 2002; Uversky et al., 2002). Large increases in the rate of self-assembly of HIV capsid protein (del Alamo et al., 2005).  
Deceleration of rapid (diffusion limited) protein associations (Zimmerman and Minton, 1993).   Reduction in rate of diffusion-limited association of TEM and BLIP (Kozer and Schreiber, 2004).  
Stabilization of proteins against denaturation by heat or chaotropes (Cheung et al., 2005; Minton, 2000a).   Elevated temperatures for half-denaturation of actin (Tellam et al., 1983) and lysozyme (Sasahara et al., 2003). Elevated urea concentration for half-denaturation of FK-506-binding protein (Spencer et al., 2005). Partial restoration of catalytic activity of ribonuclease in the presence of high urea concentration (Tokuriki et al., 2004).  
Acceleration of protein refolding to the native state (Cheung et al., 2005).   
Enhancement of aggregation of proteins that are partially or fully denatured (Hall and Minton, 2002; Hall and Minton, 2004).   Proteins that refold spontaneously in dilute solution aggregate in crowded solution and require chaperones to refold (Martin, 2002; van den Berg et al., 1999).  
Predicted effect Relevant observations§
Enhancement of equilibrium association of dilute macromolecules (Minton, 1981; Nichol et al., 1981).   Large enhancement in the extent of sickle hemoglobin polymerization (Bookchin et al., 1999); large increase in affinity of DNA-binding proteins for DNA (Zimmerman and Harrison, 1987; Jarvis et al., 1990); enhanced self-association of spectrin (Lindner and Ralston, 1995), actin (Lindner and Ralston, 1997), fibrinogen (Rivas et al., 1999), tubulin (Rivas et al., 1999) and FtsZ (Rivas et al., 2001).  
Acceleration of slow (transition state limited) protein associations (Minton, 1983; Minton, 2001a).   Large increases in the rate of fiber formation by sickle cell hemoglobin (Rotter et al., 2005), actin (Drenckhahn and Pollard, 1986), tubulin (Herzog and Weber, 1978) and fibrin (Wilf et al., 1985). Large increases in the rate of amyloid formation by apoCII (Hatters et al., 2002) and α-synuclein (Shtilerman et al., 2002; Uversky et al., 2002). Large increases in the rate of self-assembly of HIV capsid protein (del Alamo et al., 2005).  
Deceleration of rapid (diffusion limited) protein associations (Zimmerman and Minton, 1993).   Reduction in rate of diffusion-limited association of TEM and BLIP (Kozer and Schreiber, 2004).  
Stabilization of proteins against denaturation by heat or chaotropes (Cheung et al., 2005; Minton, 2000a).   Elevated temperatures for half-denaturation of actin (Tellam et al., 1983) and lysozyme (Sasahara et al., 2003). Elevated urea concentration for half-denaturation of FK-506-binding protein (Spencer et al., 2005). Partial restoration of catalytic activity of ribonuclease in the presence of high urea concentration (Tokuriki et al., 2004).  
Acceleration of protein refolding to the native state (Cheung et al., 2005).   
Enhancement of aggregation of proteins that are partially or fully denatured (Hall and Minton, 2002; Hall and Minton, 2004).   Proteins that refold spontaneously in dilute solution aggregate in crowded solution and require chaperones to refold (Martin, 2002; van den Berg et al., 1999).  
§

Additional relevant observations reported prior to 2003 have been compiled in Minton, 1983; Zimmerman and Minton, 1993; Minton, 2001a; Hall & Minton, 2003.

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