Electron microscopy articles within Nature Chemistry

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  • Article
    | Open Access

    Understanding how membrane-bound styrene oxide isomerase (SOI) catalyses the Meinwald rearrangement—a Lewis-acid-catalysed isomerization of an epoxide to a carbonyl compound—can be useful as SOI represents a green alternative to chemical synthesis. Here, the catalytic mechanism of SOI was determined using cryo-EM, EPR spectroscopy, mutagenesis, functional assays and docking experiments.

    • Basavraj Khanppnavar
    • , Joel P. S. Choo
    •  & Xiaodan Li

  • Article
    | Open Access

    The human ATP-hydrolysing enzyme p97 populates a metastable reaction intermediate, the ADP·Pi state, which is poised between hydrolysis and product release. Now, molecular motions at the active site in the temporal window immediately before and after ATP hydrolysis have been elucidated by merging cryo-EM, NMR spectroscopy and molecular dynamics simulations.

    • Mikhail Shein
    • , Manuel Hitzenberger
    •  & Anne K. Schütz

  • Article
    | Open Access

    Genetic code expansion to incorporate non-α-amino acid monomers is limited by predictability of monomer reactivities in the context of the ribosome. Now the use of metadynamics simulations of pre-attack monomers in the ribosomal peptidyl transferase centre provides insight on whether an A-site monomer is likely to be reactive.

    • Zoe L. Watson
    • , Isaac J. Knudson
    •  & Ara M. Abramyan

  • Article
    | Open Access

    Proteins rich in phenylalanine-glycine (FG) repeats can phase separate through FG–FG interactions. The molecular interactions of an important FG-repeat protein, nucleoporin 98, have now been studied in liquid-like transient and amyloid-like cohesive states. These interactions underlie the behaviour of FG-repeat proteins and their function in physiological and pathological cell activities.

    • Alain Ibáñez de Opakua
    • , James A. Geraets
    •  & Markus Zweckstetter

  • Article
    | Open Access

    Most proteins must fold co-translationally on the ribosome to adopt biologically active conformations, yet structural, mechanistic descriptions are lacking. Using 19F NMR spectroscopy to study a nascent multi-domain protein has now enabled the identification of two co-translational folding intermediates that are significantly more stable than intermediates formed off the ribosome, suggesting that the ribosome may thermodynamically regulate folding.

    • Sammy H. S. Chan
    • , Tomasz Włodarski
    •  & John Christodoulou

  • Article |

    Symmetrical protein oligomers perform key structural and catalytic functions in nature, but engineering such oligomers synthetically is challenging. Now, oppositely supercharged synthetic variants of normally monomeric proteins have been shown to assemble via specific, introduced electrostatic contacts into symmetrical, highly well-defined oligomers.

    • Anna J. Simon
    • , Yi Zhou
    •  & Andrew D. Ellington

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