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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Adenosine Triphosphate / chemistry
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Crystallography, X-Ray
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DNA, Cruciform
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DNA, Single-Stranded / chemistry
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Fluorescence Resonance Energy Transfer
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Lipid Bilayers / chemistry
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Mitochondrial Proton-Translocating ATPases / chemistry
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Models, Molecular
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Molecular Conformation
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Nucleic Acid Conformation
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Protein Conformation
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Proton-Translocating ATPases / chemistry
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RNA / chemistry
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RNA, Catalytic / chemistry
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RNA, Transfer / chemistry
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Ribosomes / chemistry
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Spectrophotometry
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Structure-Activity Relationship
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Time Factors
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Tomography, Emission-Computed, Single-Photon / methods*
Substances
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DNA, Cruciform
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DNA, Single-Stranded
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Lipid Bilayers
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RNA, Catalytic
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RNA
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Adenosine Triphosphate
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RNA, Transfer
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Mitochondrial Proton-Translocating ATPases
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Proton-Translocating ATPases