Applications of time-resolved resonance energy transfer measurements in studies of the molecular crowding effect

Journal of Molecular Recognition : JMR
Varda IttahE Haas

Abstract

The native structures of many globular proteins are only weakly stabilized and form in solution ensembles of multiple conformers. The energy differences between the conformers are assumed to be small. This is the case of flexible multidomain proteins where domain motions were observed. High concentrations of inert macrosolute, which create a crowded or confined environment, can cause shifts of the distribution of the conformers of such proteins towards the more compact structures. This effect may also promote compact structures in partially folded proteins. Time-resolved dynamic non-radiative excitation energy transfer (tr-RET) is suitable for detection of either subtle or major changes in distributions of intramolecular distances in protein molecules in solutions. Two experiments were performed which demonstrated the applicability of tr-RET for detection of the effect of macrosolutes on the conformational ensembles of flexible states of protein molecules. The distribution of distances between residues 203 and 169 in the CORE domain of E. coli adenylate kinase (AK) in the denatured state was determined in the presence of high concentrations of dextran 40. A significant shift of the mean of the distribution was observed without ...Continue Reading

Citations

Jul 29, 2010·Journal of the American Chemical Society·Jiang Hong, Lila M Gierasch
Jun 25, 2008·Annual Review of Biophysics·Huan-Xiang ZhouAllen P Minton
Mar 15, 2006·Annals of the New York Academy of Sciences·Weihua GuoR Stephen Berry
Feb 25, 2014·Biophysical Journal·Huan-Xiang Zhou, Osman Bilsel
Dec 7, 2018·Chembiochem : a European Journal of Chemical Biology·Birgit Köhn, Michael Kovermann
Jan 24, 2009·Langmuir : the ACS Journal of Surfaces and Colloids·Weican ZhangPeiji Gao

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