Customize Consent Preferences

We use cookies to help you navigate efficiently and perform certain functions. You will find detailed information about all cookies under each consent category below.

The cookies that are categorized as "Necessary" are stored on your browser as they are essential for enabling the basic functionalities of the site. ... 

Always Active

Necessary cookies are required to enable the basic features of this site, such as providing secure log-in or adjusting your consent preferences. These cookies do not store any personally identifiable data.

No cookies to display.

Functional cookies help perform certain functionalities like sharing the content of the website on social media platforms, collecting feedback, and other third-party features.

No cookies to display.

Analytical cookies are used to understand how visitors interact with the website. These cookies help provide information on metrics such as the number of visitors, bounce rate, traffic source, etc.

No cookies to display.

Performance cookies are used to understand and analyze the key performance indexes of the website which helps in delivering a better user experience for the visitors.

No cookies to display.

Advertisement cookies are used to provide visitors with customized advertisements based on the pages you visited previously and to analyze the effectiveness of the ad campaigns.

No cookies to display.

Chirlmin Joo Lab presents super-sensitive identification of proteins

In biology, proteins are the hands and feet of a cell, and they play a crucial role in numerous diseases. Up to now, proteins have been identified by cutting them up into small pieces and figuring out the original protein from there.

Researchers at the Chirlmin Joo Lab (Faculty of Applied Sciences) presented a new method in Nature Nanotechnology that identifies proteins without cutting them up and which is also ultra-sensitive. Because the recognition is so specific, a very low concentration of a protein in a soup of other biomolecules is sufficient for identification.

Promising

The method is called FRET X read-more-closed and consists of a clever combination of techniques. Various DNA fragments with fluorescent labels attach to particular parts (amino acids) of the protein. The relevant positions can be determined through a microscope. It is not necessary to map the entire protein to identify it. As with DNA identification, a few markers and a database of the known proteins suffice for a match.

‘This technique has the potential to open up new possibilities for proteomics read-more-closed and for diagnoses based on biomarkers’, writes the journal GEN. In short, a promising technique that is expected to have an impact in both labs and clinics.

Eiwit identificatie met FRET-X
A protein with the code of amino acids in the background. FRET X technology identifies proteins by their fingerprints, shown here by the Cs and Ks that light up between the blue letters. (Image: Chirlmin Joo Lab, TU Delft)
The researchers visualised the principle of recognition in a one-minute video.

Comments are closed.