Spectroscopy Methods

Circular Dichroism (CD)

Description
UV CD is an excellent technique for studying the conformations adopted by proteins and nucleic acids in solution. The far-UV CD spectrum is sensitive to the peptide bond conformation and as a consequence reflects the secondary structure of the protein (alpha-helix, beta-sheet, turn and unordered content). The near-UV CD spectrum (between 320 nm and 250 nm) leads to a signal sensitive to the tertiary structure derived from Trp or Tyr. Information on secondary and tertiary structure elements of proteins can therefore be provided in a variety of experimental conditions.

Service provider
Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP),
Centro di Risonanze Magnetiche 

Location
Sesto Fiorentino, Italy

Contacts
Scientific contact: Lucia Banci
Technical contact: Rebecca Del Conte

Electron paramagnetic resonance (EPR)

Description
EPR is used for the detection and identification of free radicals and paramagnetic metal centers by measuring the absorption of electromagnetic radiation.

Service provider
Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP),
Centro di Risonanze Magnetiche 

Location
Sesto Fiorentino, Italy

Contacts
Scientific contact: Lucia Banci
Technical contact: Rebecca Del Conte

Fluorimetry

Description
Fluorimetry is a tool for protein folding/unfolding studies. Tyrosine and tryptophan are used experimentally as protein fluorescent probes, because they give a good fluorescence signal. Therefore, this technique requires proteins having either Trp or Tyr or both.

Service provider
Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP),
Centro di Risonanze Magnetiche 

Location
Sesto Fiorentino, Italy

Contacts
Scientific contact: Lucia Banci
Technical contact: Rebecca Del Conte

Stopped-flow

Description
A 2-syringe-stopped-flow device is available to measure fast kinetic processes such as protein folding, and fast reactions such as electron transfer.

Service provider
Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP),
Centro di Risonanze Magnetiche 

Location
Sesto Fiorentino, Italy

Contacts
Scientific contact: Lucia Banci
Technical contact: Rebecca Del Conte

UV-visible spectrophotometers

Description
UV-visible analysis permits the characterization of proteins coordinating several types of co-factors. The analysis of interactions between proteins exchanging cofactors can also be carried out.

Service provider
Consorzio Interuniversitario Risonanze Magnetiche di Metallo Proteine (CIRMMP),
Centro di Risonanze Magnetiche 

Location
Sesto Fiorentino, Italy

Contacts
Scientific contact: Lucia Banci
Technical contact: Rebecca Del Conte

 

 

 

 

 

 

 

This project receives funding from the European Union’s Horizon 2020 research and innovation programme under grant agreement No 654248.

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