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Structure. 2006 Apr;14(4):633-43.

Bridging conformational dynamics and function using single-molecule spectroscopy.

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1
Department of Physics, University of Illinois, Urbana-Champaign, Urbana, Illinois 61801, USA.

Abstract

In a typical structure-function relation study, the primary structure of proteins or nucleic acids is changed by mutagenesis and its functional effect is measured via biochemical means. Single-molecule spectroscopy has begun to give a whole new meaning to the "structure-function relation" by measuring the real-time conformational changes of individual biological macromolecules while they are functioning. This review discusses a few recent examples: untangling internal chemistry and conformational dynamics of a ribozyme, branch migration landscape of a Holliday junction at a single-step resolution, tRNA selection and dynamics in a ribosome, repetitive shuttling and snapback of a helicase, and discrete rotation of an ATP synthase.

PMID:
16615904
DOI:
10.1016/j.str.2006.02.005
[Indexed for MEDLINE]
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