Размер шрифта A A A Обычная версия сайта
    E-mail address:

    Laboratory for Advanced Studies of Membrane Proteins

    Our laboratory is focused on structural and biophysical studies of membrane proteins, such as ion channels, transporters, photoactive proteins, G protein-coupled receptors (GPCRs), transmembrane enzymes and their complexes. Membrane proteins play a crucial role in many physiological processes mainly involved in signal transduction and membrane transport. Their dysfunction leads to many severe health disorders such as various types of cancer, chronic inflammations, cardiovascular diseases, neurodegenerative disorders. High resolution structures of these proteins are of great importance for understanding underlying mechanisms of these diseasesand to develop rational approaches to cure them. Despite the high importance there is still no structural information for a majority of membrane proteins existing, mainly because they are difficult to handle due to their amphiphilic nature and low stability.  

    In our lab we established the infrastructure to purify and stabilize proteins from heterologous expression systems, such as E. coli, cell free and baculovirus expression systems. A variety of biophysical methods are available for structural and spectroscopic investigations of these protein systems. One of the core methods is the X-ray crystallography of membrane proteins. For this purpose we have setup a unique equipment for high throughput in meso crystallization, crystal imaging and crystallization process investigations. A Rigaku X-Ray HighFlux HomeLab is an important facility in use to characterize the quality of crystals and of proteins in solution. Advantages of modern fluorescence microscopy methods (including CLSM with Spectral Imaging, TIRFM, FCS, FCCS, 2PFM, FLIM, FRAP, SIM, PALM, direct STORM) realized in the Light Nanoscope facility is utilized for investigations of the dynamic properties of proteins and their behavior in a cellular environment. Protein targets can be further characterized with Brucker Ultraflextreme Mass Spectrometry, analytical HPLC system and differential fluorimetry to study protein thermostability.

    Superviser: Prof. Dr. Georg Büldt 
    Vice-Head: Dr. Valentin Borshchevskiy
    Web-site: http://biomrc.org/
    If you noticed a typo select it and press Ctrl+Enter.

    © 2001-2021 Московский физико-технический институт (национальный исследовательский университет)

    Противодействие коррупции | Сведения о доходах

    Политика обработки персональных данных МФТИ

    Website administration | API

    All MIPT news stories republished on third-party sites must include a citation of "MIPT News Office" that links to the original story on the MIPT site.

    MIPT in social networks