A method for rapid high-throughput biophysical analysis of proteins

By Albert Perez-Riba, L. Itzhaki. 2017

19 citations recorded by the source corpus.

Quantitative determination of protein thermodynamic stability is fundamental to many research areas, both basic and applied. Although chemical-induced denaturation is the gold-standard method, it has been replaced in many settings by semi-quantitative approaches such as thermal stability measurements. The reason for this shift is that chemical denaturation experiments are labour-intensive, sample-costly and time-consuming, and it has been assumed that miniaturisation to a high-throughput format would not be possible without concomitantly comprising data quality. Here we exploit current technologies to create a high-throughput label-free chemical denaturation method that is capable of generating replicate datasets on multiple proteins in parallel on a timescale that is at least ten times faster, much more economical on sample, and with the potential for superior data quality, than the conventional methods used in most research labs currently.

Subfields: Materials Chemistry, Molecular Biology, Spectroscopy

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Materials Chemistry

1. Carles Corbi-Verge
2. Alexey Strokach
3. Philip M. Kim
4. David Becerra
5. Albert Perez-Riba

In Molecular Biology

1. Alexey Strokach
2. Carles Corbi-Verge
3. David Becerra
4. Albert Perez-Riba
5. Philip M. Kim

In Spectroscopy

1. Carles Corbi-Verge
2. Alexey Strokach
3. David Becerra
4. Albert Perez-Riba
5. Philip M. Kim

Citations in the corpus

• Fast and flexible design of novel proteins using graph neural networks (2019, methodology): “Proteins were eluted using PBS buffer with 500 mM imidazole and dialyzed against PBS ( 51 ).”