Zobrazeno 1 - 7
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pro vyhledávání: '"Michelle K. Quinn"'
Publikováno v:
The Journal of chemical physics. 158(1)
Phase transitions of proteins are strongly influenced by surface chemical modifications or mutations. Human γD-crystallin (HGD) single-mutants have been extensively studied because they are associated with the onset of juvenile cataract. However, th
Autor:
Susan James, Michelle K. Quinn, Patrick Charbonneau, Irem Altan, Amir R. Khan, Jennifer J. McManus
Publikováno v:
Biophys J
Protein crystal production is a major bottleneck in the structural characterization of proteins. To advance beyond large-scale screening, rational strategies for protein crystallization are crucial. Understanding how chemical anisotropy (or patchines
Publikováno v:
Integrative Biology. 9:444-450
The self-assembly of proteins has been widely studied in controlled in vitro conditions, and more recently in biological environments. The self-assembly of proteins in biology can be a feature of the pathogenesis of protein condensation disease, or c
Autor:
Amir R. Khan, Jennifer J. McManus, Irem Altan, Patrick Charbonneau, Michelle K. Quinn, Susan James
Inverted solubility--a crystal melting upon cooling--is observed in a handful of proteins, such as carbomonoxy hemoglobin and $\gamma$D-crystallin. In human $\gamma$D-crystallin, the phenomenon is associated with the mutation of the 23$^\mathrm{rd}$
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec8ec0f824b41a9272eb5beb99698f07
https://mural.maynoothuniversity.ie/13458/
https://mural.maynoothuniversity.ie/13458/
The chemical modification of proteins is at the frontier of developments in biological imaging and biopharmaceutics. With the advent of more sensitive and higher resolution imaging techniques, researchers increasingly rely on the functionalization of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dd0b3cd4e6db360b1c4c2a005002d13
http://mural.maynoothuniversity.ie/13456/
http://mural.maynoothuniversity.ie/13456/
Publikováno v:
Physical Chemistry Chemical Physics. 17:5413-5420
The ability to control the self-assembly of biological molecules to form defined structures, with a high degree of predictability is a central aim for soft matter science and synthetic biology. Several examples of this are known for synthetic systems
Autor:
Emanuela Zaccarelli, Andrea Ninarello, Michelle K. Quinn, Susan James, Jennifer J. McManus, Francesco Sciortino, Nicoletta Gnan
Publikováno v:
PCCP. Physical chemistry chemical physics
17 (2015): 31177–31187. doi:10.1039/c5cp04463d
info:cnr-pdr/source/autori:M.K. Quinn (a); N. Gnan (b); S. James (a); A. Ninarello (c); F. Sciortino (b,c); E. Zaccarelli (b,c); J.J. McManus (a)/titolo:How fluorescent labelling alters the solution behaviour of proteins/doi:10.1039%2Fc5cp04463d/rivista:PCCP. Physical chemistry chemical physics (Print)/anno:2015/pagina_da:31177/pagina_a:31187/intervallo_pagine:31177–31187/volume:17
17 (2015): 31177–31187. doi:10.1039/c5cp04463d
info:cnr-pdr/source/autori:M.K. Quinn (a); N. Gnan (b); S. James (a); A. Ninarello (c); F. Sciortino (b,c); E. Zaccarelli (b,c); J.J. McManus (a)/titolo:How fluorescent labelling alters the solution behaviour of proteins/doi:10.1039%2Fc5cp04463d/rivista:PCCP. Physical chemistry chemical physics (Print)/anno:2015/pagina_da:31177/pagina_a:31187/intervallo_pagine:31177–31187/volume:17
A complete understanding of the role of molecular anisotropy in directing the self assembly of colloids and proteins remains a challenge for soft matter science and biophysics. For proteins in particular, the complexity of the surface at a molecular