Bridging conformational dynamics and function using single-molecule spectroscopy

Structure. 2006 Apr;14(4):633-43. doi: 10.1016/j.str.2006.02.005.


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

  • Research Support, N.I.H., Extramural

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Crystallography, X-Ray
  • DNA, Cruciform
  • DNA, Single-Stranded / chemistry
  • Fluorescence Resonance Energy Transfer
  • Lipid Bilayers / chemistry
  • Mitochondrial Proton-Translocating ATPases / chemistry
  • Models, Molecular
  • Molecular Conformation
  • Nucleic Acid Conformation
  • Protein Conformation
  • Proton-Translocating ATPases / chemistry
  • RNA / chemistry
  • RNA, Catalytic / chemistry
  • RNA, Transfer / chemistry
  • Ribosomes / chemistry
  • Spectrophotometry
  • Structure-Activity Relationship
  • Time Factors
  • Tomography, Emission-Computed, Single-Photon / methods*


  • DNA, Cruciform
  • DNA, Single-Stranded
  • Lipid Bilayers
  • RNA, Catalytic
  • RNA
  • Adenosine Triphosphate
  • RNA, Transfer
  • Mitochondrial Proton-Translocating ATPases
  • Proton-Translocating ATPases