Journal
COMPUTER PHYSICS COMMUNICATIONS
Volume 158, Issue 3, Pages 150-157Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.cpc.2004.02.001
Keywords
fluorescence resonance energy transfer; FRET; protein structure; structural fluctuations; structure determination; distance constraints; molecular conformation
Ask authors/readers for more resources
Fluorescence energy transfer (FRET) experiments of site-specifically labelled proteins allow one to determine distances between residues at the single molecule level, which provide information on the three-dimensional structural dynamics of the biomolecule. To systematically extract this information from the experimental data, we describe a program that generates an ensemble of configurations of residues in space that agree with the experimental distances between these positions. Furthermore, a fluctuation analysis allows to determine the structural accuracy from the experimental error.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available