Naslov
Studying Proteomics with Microcalorimetry

Autori
McGann, Matthew ; Šupljika, Filip ; Carrington, Steve

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Advances in Proteomics and Progress in Precision Medicine / - , 2018, 52-52

Skup
The 12th Central and Eastern European Proteomic Conference

Mjesto i datum
Bukurešt, Rumunjska, 24.10.2018. - 26.10.2018

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
microcalorimetry, proteomics, biomolecular interactions

Sažetak
Essentially all biological processes involve inter- and intramolecular interactions. The forces involved in these interactions are quantitated by thermodynamic parameters. Beyond thermodynamics, binding kinetics also provide a measure of the strength and nature of these interactions, which is critical to understanding the complete structure-function description of biomolecular interactions. Microcalorimetry is an ultrasensitive technique that provides direct observations of thermal changes in a sample during these interactions. Differential scanning calorimetry (DSC) is used to study intramolecular interactions, such as protein unfolding and stability. Isothermal Titration Calorimetry (ITC) measures the enthalpy change, binding affinity, and stoichiometry of an intermolecular binding reaction, such as a protein-ligand or antibody- antigen interaction. This presentation will outline how these techniques are used in basic research, and drug discovery and development. We will also discuss how the data from these techniques can be combined with other biophysical characterization tools to better understand the implications of these properties on your research.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

Napomena
Malvern Panalytical Inc.

POVEZANOST RADA