Stabilization of Proteins in Confined Spaces

by: HX Zhou, KA Dill

Biochemistry, Vol. 40, No. 38. (25 September 2001), pp. 11289-11293.

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DOI, American Chem. Soc. Publications

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Abstract

Abstract: We present theory showing that confining a protein to a small inert space (a "cage") should stabilize the protein against reversible unfolding. Examples of such spaces might include the pores within chromatography columns, the Anfinsen cage in chaperonins, the interiors of ribosomes, or regions of steric occlusion inside cells. Confinement eliminates some expanded configurations of the unfolded chain, shifting the equilibrium from the unfolded state toward the native state. The partition coefficient for a protein in a confined space is predicted to decrease significantly when the solvent is changed from native to denaturing conditions. Small cages are predicted to increase the stability of the native state by as much as 15 kcal/mol. Confinement may also increase the rates of protein or RNA folding.

@article{citeulike:2924392, abstract = {Abstract: We present theory showing that confining a protein to a small inert space (a "cage") should stabilize the protein against reversible unfolding. Examples of such spaces might include the pores within chromatography columns, the Anfinsen cage in chaperonins, the interiors of ribosomes, or regions of steric occlusion inside cells. Confinement eliminates some expanded configurations of the unfolded chain, shifting the equilibrium from the unfolded state toward the native state. The partition coefficient for a protein in a confined space is predicted to decrease significantly when the solvent is changed from native to denaturing conditions. Small cages are predicted to increase the stability of the native state by as much as 15 kcal/mol. Confinement may also increase the rates of protein or RNA folding.}, address = {Department of Physics, Drexel University, Philadelphia, Pennsylvania 19104, and Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94118}, author = {Zhou, H. X. and Dill, K. A. }, citeulike-article-id = {2924392}, doi = {http://dx.doi.org/10.1021/bi0155504}, journal = {Biochemistry}, keywords = {denaturation, proteins}, month = {September}, number = {38}, pages = {11289--11293}, posted-at = {2008-06-24 22:26:07}, priority = {2}, title = {Stabilization of Proteins in Confined Spaces}, url = {http://dx.doi.org/10.1021/bi0155504}, volume = {40}, year = {2001} }

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TY - JOUR ID - citeulike:2924392 L3 - citeulike-article-id:2924392 TI - Stabilization of Proteins in Confined Spaces JF - Biochemistry VL - 40 IS - 38 SP - 11289 EP - 11293 AD - Department of Physics, Drexel University, Philadelphia, Pennsylvania 19104, and Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94118 N2 - Abstract: We present theory showing that confining a protein to a small inert space (a "cage") should stabilize the protein against reversible unfolding. Examples of such spaces might include the pores within chromatography columns, the Anfinsen cage in chaperonins, the interiors of ribosomes, or regions of steric occlusion inside cells. Confinement eliminates some expanded configurations of the unfolded chain, shifting the equilibrium from the unfolded state toward the native state. The partition coefficient for a protein in a confined space is predicted to decrease significantly when the solvent is changed from native to denaturing conditions. Small cages are predicted to increase the stability of the native state by as much as 15 kcal/mol. Confinement may also increase the rates of protein or RNA folding. KW - denaturation KW - proteins AU - Zhou, HX AU - Dill, KA PY - 2001/09/25/ UR - http://dx.doi.org/10.1021/bi0155504 ER -

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