Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Benjamin S. Hanson"'
Autor:
Matt D. G. Hughes, Sophie Cussons, Benjamin S. Hanson, Kalila R. Cook, Tímea Feller, Najet Mahmoudi, Daniel L. Baker, Robert Ariëns, David A. Head, David J. Brockwell, Lorna Dougan
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-11 (2023)
Abstract Fibrous networks constructed from high aspect ratio protein building blocks are ubiquitous in nature. Despite this ubiquity, the functional advantage of such building blocks over globular proteins is not understood. To answer this question,
Externí odkaz:
https://doaj.org/article/75078bc47eed4e7291592f100c7a7a87
Autor:
Albert Solernou, Benjamin S Hanson, Robin A Richardson, Robert Welch, Daniel J Read, Oliver G Harlen, Sarah A Harris
Publikováno v:
PLoS Computational Biology, Vol 14, Iss 3, p e1005897 (2018)
Fluctuating Finite Element Analysis (FFEA) is a software package designed to perform continuum mechanics simulations of proteins and other globular macromolecules. It combines conventional finite element methods with stochastic thermal noise, and is
Externí odkaz:
https://doaj.org/article/a71118a522374f9194c42af343e1b282
Autor:
Matt D. G. Hughes, Lorna Dougan, Benjamin S. Hanson, Najet Mahmoudi, Sophie Cussons, David J. Brockwell
Publikováno v:
ACS Nano
Hierarchical assemblies of proteins exhibit a wide-range of material properties that are exploited both in nature and by artificially by humankind. However, little is understood about the importance of protein unfolding on the network assembly, sever
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe0effd1981642b0a6201d34de922ba5
https://doi.org/10.1021/acsnano.1c00353
https://doi.org/10.1021/acsnano.1c00353
Autor:
Lorna Dougan, Benjamin S. Hanson
Globular protein hydrogels are an emerging class of materials with the potential for rational design, and a generalized understanding of how their network properties emerge from the structure and dynamics of the building block is a key challenge. Her
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29a3a5c0b98dbf91b2548320155568e3
https://doi.org/10.1101/2021.06.01.446578
https://doi.org/10.1101/2021.06.01.446578
Many biophysical systems and proteins undergo mesoscopic conformational changes in order to perform their biological function. However, these conformational changes often result from a cascade of atomistic interactions within a much larger overall ob
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::84d25b8236c42280f729bb5652da4388
https://doi.org/10.1101/2020.11.17.386524
https://doi.org/10.1101/2020.11.17.386524
Flagellar dyneins are the molecular motors responsible for producing the propagating bending motions of cilia and flagella. They are located within a densely packed and highly organised super-macromolecular cytoskeletal structure known as the axoneme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8dbb5d47660d55bfc735d7155b1adb8
https://eprints.whiterose.ac.uk/164279/1/AxoDyneinFullAccess_Manuscript.pdf
https://eprints.whiterose.ac.uk/164279/1/AxoDyneinFullAccess_Manuscript.pdf
Hierarchical structure and mechanics are crucial in biological systems as they allow for smaller molecules, such as proteins and sugars, to be used in the construction of large scale biological structures exhibiting properties such as structural supp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3367f20e72727d3eeb848376923b18dc
https://eprints.whiterose.ac.uk/157111/7/Hanson_2020_Phys._Educ._55_025015.pdf
https://eprints.whiterose.ac.uk/157111/7/Hanson_2020_Phys._Educ._55_025015.pdf
Autor:
Cecilia Tognoloni, Sarah A. Harris, Robert Ford, Karen J. Edler, Alison Rodger, Claire E. Broughton, David I. Roper, Timothy R. Dafforn, Rosemary A. Parslow, Benjamin S. Hanson, Richard F. Collins, Yu-pin Lin, Ann E. Terry, Sarah C. Lee, Corinne J. Smith, Mohammed Jamshad
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-16 (2019)
Scientific Reports
Scientific Reports
The E. coli membrane protein ZipA, binds to the tubulin homologue FtsZ, in the early stage of cell division. We isolated ZipA in a Styrene Maleic Acid lipid particle (SMALP) preserving its position and integrity with native E. coli membrane lipids. D
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05a274d4d2df2cfeb7f0eb30a1e1abed
http://wrap.warwick.ac.uk/130959/1/WRAP-nano-encapsulated-divisome-anchor-complex-FtsZ-Roper-2019.pdf
http://wrap.warwick.ac.uk/130959/1/WRAP-nano-encapsulated-divisome-anchor-complex-FtsZ-Roper-2019.pdf
Biological organisms make use of hierarchically organised structures to modulate mechanical behaviour across multiple lengthscales, allowing microscopic objects to generate macroscopic effects. Within these structural hierarchies, the resultant physi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::716cb3b9d30b489bbd266cf62b42e3a5
https://eprints.whiterose.ac.uk/152139/1/gdpRevised.pdf
https://eprints.whiterose.ac.uk/152139/1/gdpRevised.pdf
Autor:
Genji Kurisu, Sarah A. Harris, Haruki Nakamura, Oliver G. Harlen, Benjamin S. Hanson, Daniel Read, Shinji Iida
Publikováno v:
Methods (San Diego, Calif.). 185
Cytoplasmic dynein is responsible for intra-cellular transport in eukaryotic cells. Using Fluctuating Finite Element Analysis (FFEA), a novel algorithm that represents proteins as continuum viscoelastic solids subject to thermal noise, we are buildin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8a79cb70689fd06c7ba1fafa6614a54
https://pubmed.ncbi.nlm.nih.gov/32007556
https://pubmed.ncbi.nlm.nih.gov/32007556