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Showing 1–17 of 17 results
Advanced filters: Author: Po-Ssu Huang Clear advanced filters

  • Despite substantial effort, the de novo design of a stable TIM-barrel protein fold has remained elusive. A Rosetta-based computational strategy identifies a unique 184-residue sequence that adopts a TIM-barrel structure, as revealed by X-ray crystallography.

    • Po-Ssu Huang
    • Kaspar Feldmeier
    • David Baker
    Research
    Nature Chemical Biology
    Volume: 12, P: 29-34

  • Rational protein design to achieve a given protein backbone conformation is needed to engineer specific functions. Here Anand et al. describe a machine learning method using a learned neural network potential for fixed-backbone protein design.

    • Namrata Anand
    • Raphael Eguchi
    • Po-Ssu Huang
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-11

  • In this study, 83 proteins containing helix–loop–helix–loop repeats were designed—with sequences unrelated to known repeat proteins—and experimentally characterized; 43 solution X-ray scattering spectra and 15 structures of the designed proteins show that these non-natural repeat proteins have a broad range of curvatures and that their overall structures are in close agreement with design models.

    • TJ Brunette
    • Fabio Parmeggiani
    • David Baker
    Research
    Nature
    Volume: 528, P: 580-584

  • It is unclear how unassembled secretory pathway proteins are discriminated from misfolded ones. Here the authors combine biophysical and cellular experiments to study the folding of heterodimeric interleukin 23 and describe how ER chaperones recognize unassembled proteins and aid their assembly into protein complexes while preventing the premature degradation of unassembled units.

    • Susanne Meier
    • Sina Bohnacker
    • Matthias J. Feige
    ResearchOpen Access
    Nature Communications
    Volume: 10, P: 1-12

  • An approach for the design of protein pores is demonstrated by the computational design and subsequent experimental expression of both an ion-selective and a large transmembrane pore.

    • Chunfu Xu
    • Peilong Lu
    • David Baker
    Research
    Nature
    Volume: 585, P: 129-134

  • The elucidation of general principles for designing β-barrels enables the de novo creation of fluorescent proteins.

    • Jiayi Dou
    • Anastassia A. Vorobieva
    • David Baker
    Research
    Nature
    Volume: 561, P: 485-491

  • Computational methods for the de novo design of conformationally restricted peptides produce exceptionally stable short peptides stabilized by backbone cyclization and/or internal disulfide bonds that are promising starting points for a new generation of peptide-based drugs.

    • Gaurav Bhardwaj
    • Vikram Khipple Mulligan
    • David Baker
    Research
    Nature
    Volume: 538, P: 329-335

  • Leucine-rich repeats (LRRs) can form horseshoe-like structures with different curvatures in nature. A computational approach now allows the design of 12 new LRR proteins with precise curvatures, using defined building blocks and junction modules.

    • Keunwan Park
    • Betty W Shen
    • David Baker
    Research
    Nature Structural & Molecular Biology
    Volume: 22, P: 167-174

  • Computational design enables the generation of a chimeric construct of the RAS exchange factor SOS that is specifically activated by a small molecule. The expression of this construct in different cell types reveals distinct phosphorylation kinetics.

    • John C Rose
    • Po-Ssu Huang
    • Dustin J Maly
    Research
    Nature Chemical Biology
    Volume: 13, P: 119-126

  • The computational design of an extremely stable icosahedral self-assembling protein nanocage is presented; the icosahedron should be useful for applications ranging from calibrating fluorescence microscopy to drug delivery.

    • Yang Hsia
    • Jacob B. Bale
    • David Baker
    Research
    Nature
    Volume: 535, P: 136-139

  • Chu and colleagues discuss recent developments in de novo protein design.

    • Alexander E. Chu
    • Tianyu Lu
    • Po-Ssu Huang
    Reviews
    Nature Biotechnology
    Volume: 42, P: 203-215