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Timothy J. Knowles

Researcher at University of Birmingham

Publications -  60
Citations -  3075

Timothy J. Knowles is an academic researcher from University of Birmingham. The author has contributed to research in topics: Bacterial outer membrane & Membrane protein. The author has an hindex of 23, co-authored 53 publications receiving 2548 citations. Previous affiliations of Timothy J. Knowles include Aston University.

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Membrane proteins solubilized intact in lipid containing nanoparticles bounded by styrene maleic acid copolymer.

TL;DR: It is reported that bilayer disks formed by phospholipids and styrene maleic anhydride copolymer preserve the functional and structural integrity of alpha-helical and beta-barrel transmembrane proteins.
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Membrane protein architects: the role of the BAM complex in outer membrane protein assembly.

TL;DR: How component structures and accessory interactions of the β-barrel complex illuminate the mechanisms responsible for the biogenesis of outer membrane proteins is discussed.
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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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Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes.

TL;DR: NMR titration studies show that strands from YaeT's canonical folding substrate, PhoE, bind non‐specifically along alternating sides of its mixed β sheets, thus providing an ideal platform for helping to fold nascent outer‐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.