期刊
COMPUTER PHYSICS COMMUNICATIONS
卷 158, 期 3, 页码 150-157出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.cpc.2004.02.001
关键词
fluorescence resonance energy transfer; FRET; protein structure; structural fluctuations; structure determination; distance constraints; molecular conformation
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.
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