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Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches
Department of Physics, University of Houston, Houston, Texas 77204, USA
Department of Chemistry, Umeå University, Umeå 90187, Sweden
* Authors to whom correspondence should be addressed.
Received: 11 December 2008; in revised form: 10 February 2009 / Accepted: 12 February 2009 / Published: 13 February 2009
Abstract: How the crowded environment inside cells affects folding, stability and structures of proteins is a vital question, since most proteins are made and function inside cells. Here we describe how crowded conditions can be created in vitro and in silico and how we have used this to probe effects on protein properties. We have found that folded forms of proteins become more compact in the presence of macromolecular crowding agents; if the protein is aspherical, the shape also changes (extent dictated by native-state stability and chemical conditions). It was also discovered that the shape of the macromolecular crowding agent modulates the folding mechanism of a protein; in addition, the extent of asphericity of the protein itself is an important factor in defining its folding speed.
Keywords: Macromolecular crowding; Ficoll® 70; energy landscape theory; off-lattice model; excluded volume effect; protein folding mechanism; spectroscopy
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Samiotakis, A.; Wittung-Stafshede, P.; Cheung, M.S. Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches. Int. J. Mol. Sci. 2009, 10, 572-588.
Samiotakis A, Wittung-Stafshede P, Cheung MS. Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches. International Journal of Molecular Sciences. 2009; 10(2):572-588.
Samiotakis, Antonios; Wittung-Stafshede, Pernilla; Cheung, Margaret S. 2009. "Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches." Int. J. Mol. Sci. 10, no. 2: 572-588.