Knowledge Base
Technology
What is FIDA?
What are the first principles that FIDA is based on?
Why analyse in-solution?
How does Fida 1 detect a signal?
What are the main FIDA read-outs?
What is hydrodynamic radius?
What information can hydrodynamic radius provide?
How precise if FIDA’s hydrodynamic radius (Rh)?
What is the relationship between Rh and molecular weight?
How to measure binding affinity?
Is there any buffer restriction on Fida 1?
Is there any Ph buffer restriction to use Fida 1?
Is it possible to work in PEG (viscous liquid) Glycerol, DMSO media with FIDA?
Does viscosity impact the final Fida 1 read-out?
Is there any upper limit in terms of salt concentration?
How much time is typically needed to get a KD using the Fida 1?
Are the 96-well plates from FIDA compatible with a pipetting robot?
How are the fitting models calculated?
Can FIDA measure kinetics?
How to define affinity?
What is capmix - capillary mix?
What is premix?
Hardware
What are the sample formats available on Fida 1?
How much time is typically needed to get a KD using the Fida 1?
What is the temperature range on Fida 1?
Is there a mandatory maintenance on Fida 1?
There is water on the plate seal (due to the environment the instrument operates in). Is there a way of solving this?
How much bench space do I need? / What is the footprint?
What is the temperature control range on Fida Neo?
How to coat a capillary?
Software
Quality Control
Why measure sample viscosity?
How does the PDB Correlator work?
How to correlate Alphafold data?
Why use PDB Correlator as a QC tool?
What is sample stickiness?
What is the definition of a sticky sample when it comes to FIDA measurement?
Can FIDA identify stickiness and issues related to it?
Do sticky proteins impact the FIDA signal?
What to do when a sample is sticky?
What kind of optimization can be tested to minimize stickiness?
Does viscosity impact the final Fida 1 read-out?
What are the QC parameters directly incorporated into the software?
What is protein aggregation?
Why is my protein sample aggregating?
What types of aggregates are there and how do they show in FIDA data?
How to measure sample aggregation
How to work with sticky samples?
What Quality Control parameters are incorporated in the software?
What is the temperature control range on Fida Neo?
What formats can I exports the QC reports in?
How to check sample labelling quality?
Could over-labeling your molecule have a negative effect on FIDA measurement?
Can Fida Instruments work with noncovalent labeling?
What is the polydispersity index?
What is oligomerization?
Sample
Becoming and being a FIDA user
How to become a FIDA user?
Is the Fida 1 analysis software suite freely available to FIDA users?
How does the FIDA user community work?
Is there a mandatory maintenance on Fida 1?
Is there a licence on Fida 1 or FIDA software Suite?
Is the Fida 1 or FIDA software Suite compliant with 21 CFR part 11?
How much bench space do I need? / What is the footprint?
I have Fida 1 and would want an upgrade to Fida Neo, what are my options?
What is capmix - capillary mix?
What is premix?
Protein analysis and characterisation
What different types of protein analysis/assays can be done with FIDA technology?
How to study protein cooperativity?
How to perform a binding affinity assay?
Can FIDA measure kinetics?
What is capmix - capillary mix?
What is premix?
Consumables
After I become a user, where will be able to purchase consumables?
How many runs (measurement) can be done per capillary?
What type of capillaries are there?
What is the size of the capillary?
What types of coating are there?
How to coat a capillary?
Protein stability and storage
How to measure protein stability with Fida 1?
Can FIDA be used to measure thermal stability of proteins?
How to optimise protein storage?
How to measure protein unfolding?
How to measure protein regulation?
What is the temperature range on Fida 1?

How to measure protein unfolding?

FIDA can be used to measure the unfolding of a protein through chemical denaturation. As there is no limitation on the matrix, sample can be measured in various chemical denaturants, such as urea or GnCl, to unfold the proteins.

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