AFM Force spectroscopy data analysis
At nanometis, one of the core competencies lies in the analysis and interpretation of data obtained from force spectroscopy. Based on your experimental data, we conduct the data analysis using our technology platform and thereby achieve precise, reproducible and comparable results within a few days. nanometis will then provide a customized report of the analysis fitting your requirements.
Thanks to our technology platform we are able to analyze force spectroscopy data obtained from experiments on membrane proteins, globular proteins and other biomolecules.
Following is a list of some of the information, which can be a part of the report:
Basic analysis:
Automated filtering of good curves vs. bad curves
Automated fitting of signals
High speed curve alignment (800 curves per minute)
Accurate statistical analysis
Automated clustering of main and side peaks
Customization to experimental settings
Detection of main clusters of f-d-curves (defined by the peaks) (e.g. separation of good and bad curves)
Protein analysis:
Membrane proteins:
Combination of experimental results and existing public databases (e.g. PDB, Uniprot, Structure Prediction)
Alignment, force distribution, contour length distribution over all curves related to amino acids
Amino-acid sequence related to all curves
Clustering of experimental results to identify significant events
2-D / 3-D structure with highlighted unfolding energy barriers (e.g. significance of a certain unfolding event)
Images in 2-D membrane topology (e.g. how does it traverse the membrane and where are the helices and β-sheets)
Grayscale alignment
Peak cooccurrence analysis
Identification of unfolding pathways
Significance of side peaks, given the main peaks
Globular proteins:
Combination of experimental results and existing public databases (e.g. PDB, Uniprot, Structure Prediction)
Alignment, force distribution, contour length distribution over all curves related to amino acids
Amino-acid sequence related to for all curves
Clustering of experimental results to identify significant events
3-D structure with highlighted unfolding energy barriers
Peak cooccurrence analysis
Identification of unfolding pathways
Significance of side peaks, given the main peaks
Comparison and interpretation of results:
Interaction properties
Localization of ligand binding sites
Detection of cystein-/disulfide-bridges
Energy landscapes and topology of varying energy landscapes
Point mutations of proteins
Comparison of different experiments under varying physiological conditions (e.g. temperature, pH-value, salinity, ligands)
For specific requests, please send us an e-mail at service@nanometis.com with a short description of your required analysis and our experts will contact you shortly.