M
Mark Bycroft
Researcher at Medical Research Council
Publications - 74
Citations - 7813
Mark Bycroft is an academic researcher from Medical Research Council. The author has contributed to research in topics: Barnase & Protein structure. The author has an hindex of 41, co-authored 74 publications receiving 7515 citations. Previous affiliations of Mark Bycroft include The Chinese University of Hong Kong & University of Cambridge.
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Transient folding intermediates characterized by protein engineering
TL;DR: Kinetic experiments on engineered mutants of barnase detect an intermediate on the folding pathway and allow the mapping of the tertiary interactions of the side chains and their energetics, which provide extensive structural characterization of the folding intermediate and the sequence of events in the folded pathway.
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The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
Alex Bateman,Mark Bycroft +1 more
TL;DR: The structure of the LysM domain is determined from E. coli membrane-bound lytic murein transglycosylase D with a betaalphaalphabeta secondary structure with the two helices packing onto the same side of an anti- parallel beta sheet.
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Strength and co-operativity of contributions of surface salt bridges to protein stability
TL;DR: There is a triad of charged residues on the surface of barnase, comprising residues Asp8, Asp12 and Arg110, that interact by forming two exposed salt bridges that contribute to the stability of the protein.
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The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.
TL;DR: Enhanced sequence searches reveal hitherto unidentified S1 domains in RNase E, RNase II, NusA, EMB-5, and other proteins, suggesting that they are both derived from an ancient nucleic acid-binding protein.
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RNA recognition by a Staufen double‐stranded RNA‐binding domain
Andres Ramos,Stefan Grünert,Jan Adams,David Micklem,Mark R. Proctor,Stefan M.V. Freund,Mark Bycroft,Daniel St Johnston,Gabriele Varani +8 more
TL;DR: It is shown that the RNA‐binding activity of dsRBD3 is required in vivo for Staufen‐dependent localization of bicoid and oskar mRNAs.