![Guto Rhys](https://profiles-cardiff.imgix.net/attachments/1524?w=200&h=200&auto=format&crop=faces&fit=crop&q=90")
Trosolwyg
Mae gan labordy Rhys ddiddordeb mewn dylunio peptidau a phroteinau newydd, a pheirianneg sy'n bodoli. Mae'r datblygiadau diweddaraf mewn dulliau arbrofol ac algorithmau cyfrifiadurol yn ein galluogi i ddatblygu peptidau a phroteinau newydd nad ydynt yn bodoli ym myd natur. Rydym yn datblygu tîm o wyddonwyr rhyngddisgyblaethol iawn i fynd i'r afael â rhai o'r heriau nas diwallwyd y mae cymdeithas yn eu hwynebu. Mae'r rhain yn cynnwys datblygu therapiwteg newydd ar gyfer clefydau sy'n anodd eu trin ar hyn o bryd, ac ensymau newydd i ddisodli adweithiau cemegol sy'n ddrwg i'r amgylchedd.
Mae ein swyddfa bob amser yn agored i fentrau newydd. Mae ein labordy hefyd yn amgylchedd cefnogol sy'n gofalu am ddatblygiad ei fyfyrwyr a'i staff. Rydym yn croesawu unrhyw un, beth bynnag eu hoedran, anabledd, ethnigrwydd, rhyw a chyfeiriadedd rhywiol. Rydym yn agored i unrhyw un sydd am gyfrannu at wneud y labordy yn amgylchedd amrywiol, cynhwysol a chyfeillgar.
Am y wybodaeth ddiweddaraf, ewch i www.rhyslab.com
Cyhoeddiad
2023
- Dawson, W. M. et al. 2023. Differential sensing with arrays of de novo designed peptide assemblies. Nature Communications 14, article number: 383. (10.1038/s41467-023-36024-y)
2022
- Rhys, G. G. et al. 2022. De novo designed peptides for cellular delivery and subcellular localisation. Nature Chemical Biology 18(9), pp. 999-1004. (10.1038/s41589-022-01076-6)
2021
- Dawson, W. M. et al. 2021. Structural resolution of switchable states of a de novo peptide assembly. Nature Communications 12(1), article number: 1530. (10.1038/s41467-021-21851-8)
- Rhys, G. G., Dawson, W. M., Beesley, J. L., Martin, F. J. O., Brady, R. L., Thomson, A. R. and Woolfson, D. N. 2021. How coiled-coil assemblies accommodate multiple aromatic residues. Biomacromolecules 22(5) (10.1021/acs.biomac.1c00131)
- Dawson, W. M., Martin, F. J. O., Rhys, G. G., Shelley, K. L., Brady, R. L. and Woolfson, D. N. 2021. Coiled coils 9-to-5: rational de novo design of α-helical barrels with tunable oligomeric states. Chemical Science 12(20), pp. 6923-6928. (10.1039/D1SC00460C)
2019
- Dawson, W. M., Rhys, G. G. and Woolfson, D. N. 2019. Towards functional de novo designed proteins. Current Opinion in Chemical Biology 52, pp. 102-111. (10.1016/j.cbpa.2019.06.011)
- Boyle, A. L. et al. 2019. Selective coordination of three transition metal ions within a coiled-coil peptide scaffold. Chemical Science 10(31), pp. 7456-7465. (10.1039/C9SC01165J)
- Rhys, G. G. et al. 2019. Navigating the structural landscape of de novo α-helical bundles. Journal of the American Chemical Society 141(22), pp. 8787-8797. (10.1021/jacs.8b13354)
2018
- Rhys, G. G., Wood, C. W., Lang, E. J. M., Mulholland, A. J., Brady, R. L., Thomson, A. R. and Woolfson, D. N. 2018. Maintaining and breaking symmetry in homomeric coiled-coil assemblies. Nature Communications 9(1), article number: 4132. (10.1038/s41467-018-06391-y)
- Fletcher, J. M., Horner, K. A., Bartlett, G. J., Rhys, G. G., Wilson, A. J. and Woolfson, D. N. 2018. De novocoiled-coil peptides as scaffolds for disrupting protein–protein interactions. Chemical Science 9(39), pp. 7656-7665. (10.1039/C8SC02643B)
- Thomas, F. et al. 2018. De novo-designed α-helical barrels as receptors for small molecules. ACS Synthetic Biology 7(7), pp. 1808-1816. (10.1021/acssynbio.8b00225)
- Galloway, J. M. et al. 2018. Bioinspired silicification reveals structural detail in self-assembled peptide cages. ACS Nano 12(2), pp. 1420-1432. (10.1021/acsnano.7b07785)
Erthyglau
- Dawson, W. M. et al. 2023. Differential sensing with arrays of de novo designed peptide assemblies. Nature Communications 14, article number: 383. (10.1038/s41467-023-36024-y)
- Rhys, G. G. et al. 2022. De novo designed peptides for cellular delivery and subcellular localisation. Nature Chemical Biology 18(9), pp. 999-1004. (10.1038/s41589-022-01076-6)
- Dawson, W. M. et al. 2021. Structural resolution of switchable states of a de novo peptide assembly. Nature Communications 12(1), article number: 1530. (10.1038/s41467-021-21851-8)
- Rhys, G. G., Dawson, W. M., Beesley, J. L., Martin, F. J. O., Brady, R. L., Thomson, A. R. and Woolfson, D. N. 2021. How coiled-coil assemblies accommodate multiple aromatic residues. Biomacromolecules 22(5) (10.1021/acs.biomac.1c00131)
- Dawson, W. M., Martin, F. J. O., Rhys, G. G., Shelley, K. L., Brady, R. L. and Woolfson, D. N. 2021. Coiled coils 9-to-5: rational de novo design of α-helical barrels with tunable oligomeric states. Chemical Science 12(20), pp. 6923-6928. (10.1039/D1SC00460C)
- Dawson, W. M., Rhys, G. G. and Woolfson, D. N. 2019. Towards functional de novo designed proteins. Current Opinion in Chemical Biology 52, pp. 102-111. (10.1016/j.cbpa.2019.06.011)
- Boyle, A. L. et al. 2019. Selective coordination of three transition metal ions within a coiled-coil peptide scaffold. Chemical Science 10(31), pp. 7456-7465. (10.1039/C9SC01165J)
- Rhys, G. G. et al. 2019. Navigating the structural landscape of de novo α-helical bundles. Journal of the American Chemical Society 141(22), pp. 8787-8797. (10.1021/jacs.8b13354)
- Rhys, G. G., Wood, C. W., Lang, E. J. M., Mulholland, A. J., Brady, R. L., Thomson, A. R. and Woolfson, D. N. 2018. Maintaining and breaking symmetry in homomeric coiled-coil assemblies. Nature Communications 9(1), article number: 4132. (10.1038/s41467-018-06391-y)
- Fletcher, J. M., Horner, K. A., Bartlett, G. J., Rhys, G. G., Wilson, A. J. and Woolfson, D. N. 2018. De novocoiled-coil peptides as scaffolds for disrupting protein–protein interactions. Chemical Science 9(39), pp. 7656-7665. (10.1039/C8SC02643B)
- Thomas, F. et al. 2018. De novo-designed α-helical barrels as receptors for small molecules. ACS Synthetic Biology 7(7), pp. 1808-1816. (10.1021/acssynbio.8b00225)
- Galloway, J. M. et al. 2018. Bioinspired silicification reveals structural detail in self-assembled peptide cages. ACS Nano 12(2), pp. 1420-1432. (10.1021/acsnano.7b07785)
Addysgu
CH5110 Blwyddyn 1 Sylfaen Cemeg Ymarferol
CH4305 Macromolecules bywyd