Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10–14 June 2012)

Abstract : More than 60 years of biochemical and biophysical studies have accustomed us to think of proteins as highly purified entities that act in isolation, more or less freely diffusing until they find their cognate partner to bind to. While in vitro experiments that reproduce these conditions largely remain the only way to investigate the intrinsic properties of molecules, this approach ignores an important factor: in their natural milieu , proteins are surrounded by several other molecules of different chemical nature, and this crowded environment can considerably modify their behaviour.
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https://hal.archives-ouvertes.fr/hal-02071788
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Submitted on : Monday, March 18, 2019 - 5:01:16 PM
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G Foffi, A. Pastore, Francesco Piazza, A Temussi. Macromolecular crowding: chemistry and physics meet biology (Ascona, Switzerland, 10–14 June 2012). Physical Biology, Institute of Physics: Hybrid Open Access, 2013, 10 (4), pp.040301. ⟨10.1088/1478-3975/10/4/040301⟩. ⟨hal-02071788⟩

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