The folding dynamics of proteins at the single-molecule level has been studied with single-molecule force spectroscopy experiments for 20 years, but a common standardized method for the analysis of the collected data and for sharing among the scientific community members is still not available. We have developed a new open-source tool—Fodis—for the analysis of the force-distance curves obtained in single-molecule force spectroscopy experiments, providing almost automatic processing, analysis, and classification of the obtained data. Our method provides also a classification of the possible unfolding pathways and the structural heterogeneity present during the unfolding of proteins.
Fodis: Software for Protein Unfolding Analysis / Galvanetto, Nicola; Perissinotto, Andrea; Pedroni, Andrea; Torre, Vincent. - In: BIOPHYSICAL JOURNAL. - ISSN 0006-3495. - 114:6(2018), pp. 1264-1266. [10.1016/j.bpj.2018.02.004]
Fodis: Software for Protein Unfolding Analysis
Galvanetto, Nicola;Perissinotto, Andrea;Pedroni, Andrea;Torre, Vincent
2018-01-01
Abstract
The folding dynamics of proteins at the single-molecule level has been studied with single-molecule force spectroscopy experiments for 20 years, but a common standardized method for the analysis of the collected data and for sharing among the scientific community members is still not available. We have developed a new open-source tool—Fodis—for the analysis of the force-distance curves obtained in single-molecule force spectroscopy experiments, providing almost automatic processing, analysis, and classification of the obtained data. Our method provides also a classification of the possible unfolding pathways and the structural heterogeneity present during the unfolding of proteins.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
