Protein dynamics from single-molecule fluorescence intensity correlation functions

Single-molecule fluorescence studies of protein folding and conformational dynamics.

Exploring single-molecule dynamics with fluorescence nanoscopy

The study of molecular dynamics at the single-molecule level with fluorescence correlation spectroscopy (FCS) and far-field optics has contributed greatly to the functional understanding of complex systems. Unfortunately, such studies are restricted to length scales of >200 nm because diffraction does not allow further reduction of the measurement volume. This sets an upper limit on the applica...

Single-molecule fluorescence spectroscopy of protein folding.

Single-molecule spectroscopy is an important new approach for studying the intrinsically heterogeneous process of protein folding. This Review illustrates how different single-molecule fluorescence techniques have improved our understanding of mechanistic aspects in protein folding, exemplified by a series of recent experiments on a small protein.

Single Molecule Fluorescence Investigation of Protein Folding

Title of Document: SINGLE MOLECULE FLUORESCENCE INVESTIGATION OF PROTEIN FOLDING Jianwei Liu, Ph.D., 2008 Directed By: Associate Professor, Victor Muñoz, Department of Chemistry and Biochemistry In addition to the well known two-state folding scenario, the energy landscape theory of protein folding predicts the possibility of downhill folding under native conditions. This intriguing prediction ...

Single-molecule dynamics of phytochrome-bound fluorophores probed by fluorescence correlation spectroscopy.

Fluorescence correlation spectroscopy (FCS) was used to investigate the hydrodynamic and photophysical properties of PR1 (phytofluor red 1), an intensely red fluorescent biliprotein variant of the truncated cyanobacterial phytochrome 1 (Cph1Delta, which consists of the N-terminal 514 amino acids). Single-molecule diffusion measurements showed that PR1 has excellent fluorescence properties at th...