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Mohammed Jamshad

Researcher at University of Birmingham

Publications -  41
Citations -  1496

Mohammed Jamshad is an academic researcher from University of Birmingham. The author has contributed to research in topics: Membrane protein & Homologous recombination. The author has an hindex of 15, co-authored 39 publications receiving 1205 citations. Previous affiliations of Mohammed Jamshad include University of Warwick & Aston University.

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A method for detergent-free isolation of membrane proteins in their local lipid environment

TL;DR: This protocol describes the preparation of styrene maleic acid (SMA) co-polymer to extract membrane proteins from prokaryotic and eukaryotic expression systems and provides a practical tool kit for those wanting to use SMALPs to study membrane proteins.
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Detergent-free purification of ABC (ATP-binding-cassette) transporters

TL;DR: It is demonstrated that eukaryotic ABC transporters can be extracted and purified without ever being removed from their lipid bilayer environment, opening up a wide range of possibilities for the future study of their structure and function.
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Structural analysis of a nanoparticle containing a lipid bilayer used for detergent-free extraction of membrane proteins.

TL;DR: The structure of the SMA lipid particle (SMALP) is described using data from small angle neutron scattering, electron microscopy, and attenuated total reflection Fourier transform infrared spectroscopy to form the foundation for future development and applications of SMALPs in membrane protein production and analysis.
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G-protein coupled receptor solubilization and purification for biophysical analysis and functional studies, in the total absence of detergent

TL;DR: The first solubilization and purification of a functional GPCR [human adenosine A2A receptor (A2AR)], in the total absence of detergent at any stage, is reported, by exploiting spontaneous encapsulation by styrene maleic acid co-polymer direct from the membrane into a nanoscale SMA lipid particle (SMALP).
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Surfactant-free purification of membrane proteins with intact native membrane environment

TL;DR: A method employing the amphipathic polymer poly(styrene-co-maleic acid), which is able to reversibly encapsulate the membrane protein in a 10 nm disc-like structure ideally suited to purification and further biochemical study is examined.