Zobrazeno 1 - 10
of 57
pro vyhledávání: '"R. Leo Brady"'
Autor:
William M. Dawson, Kathryn L. Shelley, Jordan M. Fletcher, D. Arne Scott, Lucia Lombardi, Guto G. Rhys, Tania J. LaGambina, Ulrike Obst, Antony J. Burton, Jessica A. Cross, George Davies, Freddie J. O. Martin, Francis J. Wiseman, R. Leo Brady, David Tew, Christopher W. Wood, Derek N. Woolfson
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-12 (2023)
Differential sensing aims to mimic senses such as taste and smell through the use of synthetic receptors. Here, the authors show that arrays of de novo designed peptide assemblies can be used as sensor components to distinguish various analytes and c
Externí odkaz:
https://doaj.org/article/a820f403adc549ffa2b3bf2e841354ca
Autor:
William M. Dawson, Eric J. M. Lang, Guto G. Rhys, Kathryn L. Shelley, Christopher Williams, R. Leo Brady, Matthew P. Crump, Adrian J. Mulholland, Derek N. Woolfson
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
So far most of the de novo designed proteins are for single states only. Here, the authors present the de novo design and crystal structure determination of a coiled-coil peptide that assembles into multiple, distinct conformational states under the
Externí odkaz:
https://doaj.org/article/da6fbe49cbb74470820dc44739bd5079
Autor:
Guto G. Rhys, Christopher W. Wood, Eric J. M. Lang, Adrian J. Mulholland, R. Leo Brady, Andrew R. Thomson, Derek N. Woolfson
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Higher order coiled coils with five or more helices can form α-helical barrels. Here the authors show that placing β-branched aliphatic residues along the lumen yields stable and open α-helical barrels, which is of interest for the rational design
Externí odkaz:
https://doaj.org/article/5c02c52e40f94c5bb66b86f6007891f4
Autor:
Matthew L. Brewer, David Dymock, R. Leo Brady, Bernhard B. Singer, Mumtaz Virji, Darryl J. Hill
Publikováno v:
Journal of Oral Microbiology, Vol 11, Iss 1 (2019)
Neisseria meningitidis, Haemophilus influenzae, and Moraxella catarrhalis are pathogenic bacteria adapted to reside on human respiratory mucosal epithelia. One common feature of these species is their ability to target members of the carcinoembryonic
Externí odkaz:
https://doaj.org/article/7f49ede41c7144dab76ae536caa2eb74
Autor:
Kozhinjampara R. Mahendran, William M. Dawson, Mark I. Wallace, Jason T. Sengel, Adrian J. Mulholland, William F. DeGrado, Hagan Bayley, Lijun Liu, R. Leo Brady, Eric J. M. Lang, Ai Niitsu, Alistair J. Scott, Derek N. Woolfson, Marco Mravic, Andrew R. Thomson, Huong T. Kratochvil
Publikováno v:
Scott, A J, Niitsu, A, Lang, E J M, Dawson, W M, Brady, R L, Mulholland, A J & Woolfson, D N 2021, ' Constructing ion channels from water-soluble α-helical barrels ', Nature Chemistry, vol. 13, no. 7, pp. 643-650 . https://doi.org/10.1038/s41557-021-00688-0
The design of peptides that assemble in membranes to form functional ion channels is challenging. Specifically, hydrophobic interactions must be designed between the peptides and at the peptide–lipid interfaces simultaneously. Here, we take a multi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37756b89f736b22f8a11bd297b48bcde
https://doi.org/10.1038/s41557-021-00688-0
https://doi.org/10.1038/s41557-021-00688-0
Autor:
Guto G. Rhys, William M. Dawson, Derek N. Woolfson, Freddie J. O. Martin, R. Leo Brady, Kathryn L Shelley
Publikováno v:
Dawson, W M, Martin, F J O, Rhys, G G, Shelley, K L, Brady, R L & Woolfson, D N 2021, ' Coiled coils 9-to-5 : rational de novo design of α-helical barrels with tunable oligomeric states ', Chemical Science, vol. 12, no. 20, pp. 6923-6928 . https://doi.org/10.1039/d1sc00460c
The rational design of linear peptides that assemble controllably and predictably in water is challenging. Short sequences must encode unique target structures and avoid alternative states. However, the non-covalent forces that stabilize and discrimi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::939f1f7d1bd526a6bd01378f9c86571c
https://doi.org/10.1039/d1sc00460c
https://doi.org/10.1039/d1sc00460c
Autor:
Christopher Williams, William M. Dawson, Adrian J. Mulholland, Matthew P. Crump, R. Leo Brady, Eric J. M. Lang, Kathryn L Shelley, Guto G. Rhys, Derek N. Woolfson
Publikováno v:
Nature Communications
Dawson, W M, Lang, E J M, Rhys, G G, Shelley, K L, Williams, C, Brady, R L, Crump, M P, Mulholland, A J & Woolfson, D N 2021, ' Structural resolution of switchable states of a de novo peptide assembly ', Nature Communications, vol. 12, no. 1, 1530 (2020) . https://doi.org/10.1038/s41467-021-21851-8
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
Dawson, W M, Lang, E J M, Rhys, G G, Shelley, K L, Williams, C, Brady, R L, Crump, M P, Mulholland, A J & Woolfson, D N 2021, ' Structural resolution of switchable states of a de novo peptide assembly ', Nature Communications, vol. 12, no. 1, 1530 (2020) . https://doi.org/10.1038/s41467-021-21851-8
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
De novo protein design is advancing rapidly. However, most designs are for single states. Here we report a de novo designed peptide that forms multiple α-helical-bundle states that are accessible and interconvertible under the same conditions. Usual
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4412c9b6d818e92335594445134d1004
http://europepmc.org/articles/PMC7943578
http://europepmc.org/articles/PMC7943578
Autor:
William M, Dawson, Freddie J O, Martin, Guto G, Rhys, Kathryn L, Shelley, R Leo, Brady, Derek N, Woolfson
Publikováno v:
Chemical Science
The rational design of linear peptides that assemble controllably and predictably in water is challenging. Short sequences must encode unique target structures and avoid alternative states. However, the non-covalent forces that stabilize and discrimi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9912a759cb517f015177aa33c997d95e
https://pubmed.ncbi.nlm.nih.gov/34745518
https://pubmed.ncbi.nlm.nih.gov/34745518
Autor:
William M. Dawson, Freddie J. O. Martin, Derek N. Woolfson, Kathryn L Shelley, Guto G. Rhys, R. Leo Brady
The rational design of linear peptides that assemble controllably and predictably in water is challenging. Sequences must encode unique target structures and avoid alternative states. However, the stabilizing and discriminating non-covalent forces av
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::166d59cbb2f381b7920e69a53824066c
https://doi.org/10.1101/2021.01.20.427391
https://doi.org/10.1101/2021.01.20.427391
Autor:
Katherine McAuley, Jan Bieschke, Daljit Sangar, Matthew J. Cliff, Elizabeth B. Sawyer, John Collinge, Graham S. Jackson, Jonathan P. Waltho, Mark Batchelor, Rebecca Conners, R. Leo Brady, Laszlo L. P. Hosszu, Andrea M. Hounslow, Stuart Fisher
Publikováno v:
Hosszu, L L P, Conners, R, Sangar, D, Batchelor, M, Sawyer, E B, Fisher, S, Cliff, M J, Hounslow, A M, McAuley, K, Brady, R L, Jackson, G S, Bieschke, J, Waltho, J P & Collinge, J 2020, ' Structural effects of the highly protective V127 polymorphism on human prion protein ', Communications Biology . https://doi.org/10.1038/s42003-020-01126-6
Communications Biology, Vol 3, Iss 1, Pp 1-12 (2020)
Hosszu, L L P, Conners, R, Sangar, D, Batchelor, M, Sawyer, E B, Fisher, S, Cliff, M J, Hounslow, A M, McAuley, K, Brady, R L, Jackson, G S, Bieschke, J, Waltho, J P & Collinge, J 2020, ' Structural effects of the highly protective V127 polymorphism on human prion protein ', Communications Biology, vol. 3, 402 . https://doi.org/10.1038/s42003-020-01126-6
Communications Biology
Communications Biology, Vol 3, Iss 1, Pp 1-12 (2020)
Hosszu, L L P, Conners, R, Sangar, D, Batchelor, M, Sawyer, E B, Fisher, S, Cliff, M J, Hounslow, A M, McAuley, K, Brady, R L, Jackson, G S, Bieschke, J, Waltho, J P & Collinge, J 2020, ' Structural effects of the highly protective V127 polymorphism on human prion protein ', Communications Biology, vol. 3, 402 . https://doi.org/10.1038/s42003-020-01126-6
Communications Biology
Prion diseases, a group of incurable, lethal neurodegenerative disorders of mammals including humans, are caused by prions, assemblies of misfolded host prion protein (PrP). A single point mutation (G127V) in human PrP prevents prion disease, however
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::804aab64475c96d92a6f0edafe6af6be
https://doi.org/10.1038/s42003-020-01126-6
https://doi.org/10.1038/s42003-020-01126-6