Bridging Conformational Dynamics and Function Using Single-Molecule Spectroscopy

Sua Myong, Benjamin C. Stevens, Taekjip Ha

Research output: Contribution to journalReview articlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)633-643
Number of pages11
JournalStructure
Volume14
Issue number4
DOIs
StatePublished - Apr 2006

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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