Probing single-molecule protein conformational dynamics.

H Peter Lu

doi:10.1021/ar0401451

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Probing single-molecule protein conformational dynamics.

H Peter Lu

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Abstract

Protein conformational fluctuations and dynamics, often complex and associated with inhomogeneities, play a crucial role in biomolecular functions. It is extremely difficult to characterize such inhomogeneous dynamics in an ensemble-averaged measurement, especially when the proteins are involved in multiple-step, multiple-conformation complex chemical interactions and transformations, such as in enzymatic reactions, protein-protein interactions, and ion-channel membrane protein processes. Alternatively, single-molecule spectroscopy is a powerful approach to probing and analyzing protein conformational dynamics in real time.

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Bacteriophage T4 Dimerization Fluorescence Resonance Energy Transfer Gramicidin Ion Channels Lipid Bilayers Membrane Proteins Muramidase Protein Conformation Signal Transduction Spectrometry, Fluorescence Viral Proteins cdc42 GTP-Binding Protein Journal Article Research Support, U.S. Gov't, Non-P.H.S.

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H Peter Lu. 2005. Probing single-molecule protein conformational dynamics.. https://doi.org/10.1021/ar0401451

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