| Literature DB >> 29590583 |
Nicola Galvanetto1, Andrea Perissinotto2, Andrea Pedroni2, Vincent Torre3.
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.Mesh:
Year: 2018 PMID: 29590583 PMCID: PMC5883950 DOI: 10.1016/j.bpj.2018.02.004
Source DB: PubMed Journal: Biophys J ISSN: 0006-3495 Impact factor: 4.033