Abstract
Protein conformational fluctuations and dynamics, often associated with static and dynamic inhomogeneities, play a crucial role in biomolecular functions. It is extremely difficult to characterize such spatially and temporally inhomogeneous dynamics in an ensemble-averaged measurement, especially when the proteins involve in a multiple-step and multiple-conformation complex chemical interactions and transformations, such as in protein-protein interactions and protein- DNA interactions. Single-molecule spectroscopy is a powerful approach to analyze protein conformational dynamics under physiological conditions, providing dynamic perspectives on a molecular-level understanding of protein structurefunction mechanisms.
Current Pharmaceutical Biotechnology
Title: Single-Molecule Protein Interaction Conformational Dynamics
Volume: 10 Issue: 5
Author(s): H. Peter Lu
Affiliation:
Abstract: Protein conformational fluctuations and dynamics, often associated with static and dynamic inhomogeneities, play a crucial role in biomolecular functions. It is extremely difficult to characterize such spatially and temporally inhomogeneous dynamics in an ensemble-averaged measurement, especially when the proteins involve in a multiple-step and multiple-conformation complex chemical interactions and transformations, such as in protein-protein interactions and protein- DNA interactions. Single-molecule spectroscopy is a powerful approach to analyze protein conformational dynamics under physiological conditions, providing dynamic perspectives on a molecular-level understanding of protein structurefunction mechanisms.
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Cite this article as:
Lu Peter H., Single-Molecule Protein Interaction Conformational Dynamics, Current Pharmaceutical Biotechnology 2009; 10 (5) . https://dx.doi.org/10.2174/138920109788922119
DOI https://dx.doi.org/10.2174/138920109788922119 |
Print ISSN 1389-2010 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4316 |
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