Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Ashley Namini"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Intrinsically disordered proteins play key roles in regulatory protein interactions, but their detailed structural characterization remains challenging. Here we calculate and compare conformational ensembles for the disordered protein Sic1 from yeast
Externí odkaz:
https://doaj.org/article/d0b02bef31d5493c950fd75b93ab2a8d
Autor:
João M. C. Teixeira, Zi Hao Liu, Ashley Namini, Jie Li, Robert M. Vernon, Mickaël Krzeminski, Alaa A. Shamandy, Oufan Zhang, Mojtaba Haghighatlari, Lei Yu, Teresa Head-Gordon, Julie D. Forman-Kay
Publikováno v:
The journal of physical chemistry. A, vol 126, iss 35
The power of structural information for informing biological mechanisms is clear for stable folded macromolecules, but similar structure-function insight is more difficult to obtain for highly dynamic systems such as intrinsically disordered proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b316bcf30e4dd7d6786743905e3d55c9
https://doi.org/10.1021/acs.jpca.2c03726
https://doi.org/10.1021/acs.jpca.2c03726
Autor:
Jie Li, Oufan Zhang, Seokyoung Lee, Ashley Namini, Zi Hao Liu, João M. C. Teixeira, Julie D. Forman-Kay, Teresa Head-Gordon
Publikováno v:
Journal of Chemical Theory and Computation.
We consider a generic representation problem of internal coordinates (bond lengths, valence angles, and dihedral angles) and their transformation to 3-dimensional Cartesian coordinates of a biomolecule. We show that the internal-to-Cartesian process
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3a6522dcacf3112acc286215cdfcdb7
https://doi.org/10.1021/acs.jctc.2c01270
https://doi.org/10.1021/acs.jctc.2c01270
Autor:
Oufan Zhang, Mojtaba Haghighatlari, Jie Li, Zi Hao Liu, Ashley Namini, João M. C. Teixeira, Julie D. Forman-Kay, Teresa Head-Gordon
The structural characterization of proteins with a disorder requires a computational approach backed by experiments to model their diverse and dynamic structural ensembles. The selection of conformational ensembles consistent with solution experiment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6afdf56d6408b041196547e732275a30
http://arxiv.org/abs/2206.12667
http://arxiv.org/abs/2206.12667
Autor:
João M.C. Teixeira, Zi Hao Liu, Ashley Namini, Jie Li, Robert M. Vernon, Mickaël Krzeminski, Alaa A. Shamandy, Oufan Zhang, Mojtaba Haghighatlari, Lei Yu, Teresa Head-Gordon, Julie D. Forman-Kay
The power of structural information for informing biological mechanism is clear for stable folded macromolecules, but similar structure-function insight is more difficult to obtain for highly dynamic systems such as intrinsically disordered proteins
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::953785f8d5336f811aa44db303afeefb
https://doi.org/10.1101/2022.05.28.493726
https://doi.org/10.1101/2022.05.28.493726
Autor:
Pavithra M. Naullage, Mojtaba Haghighatlari, Ashley Namini, João M. C. Teixeira, Jie Li, Oufan Zhang, Claudiu C. Gradinaru, Julie D. Forman-Kay, Teresa Head-Gordon
Publikováno v:
The journal of physical chemistry. B, vol 126, iss 9
J Phys Chem B
J Phys Chem B
Intrinsically disordered proteins and unfolded proteins have fluctuating conformational ensembles that are fundamental to their biological function and impact protein folding, stability and misfolding. Despite the importance of protein dynamics and c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3785697e8c61865d87c34d0e3028f6b1
https://escholarship.org/uc/item/5g28b0tt
https://escholarship.org/uc/item/5g28b0tt
Autor:
Ashley Namini, Julie D. Forman-Kay, Mickael Krzeminski, Tanja Mittag, Claudiu C. Gradinaru, Teresa Head-Gordon, Gregory-Neal W. Gomes, Erik W. Martin
Publikováno v:
J Am Chem Soc
Journal of the American Chemical Society, vol 142, iss 37
Journal of the American Chemical Society, vol 142, iss 37
Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which makes structural characterization challenging. Although challenging, characterizing the conformational ensembles of IDPs is of great interest, since their co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd00c458f87f6f506afd24324d8a9b42
https://pubmed.ncbi.nlm.nih.gov/32840111
https://pubmed.ncbi.nlm.nih.gov/32840111
Autor:
Gregory-Neal W. Gomes, Julie D. Forman-Kay, Mickael Krzeminski, Ashley Namini, Claudiu C. Gradinaru, Teresa Head-Gordon, Tanja Mittag, Erik W. Martin
Intrinsically disordered proteins (IDPs) have fluctuating heterogeneous conformations, which makes structural characterization challenging. Although challenging, characterizing the conformational ensembles of IDPs is of great interest, since their co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4e31c0e7c8e17ebc098ff74c4e431f7