Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Sandhya Premnath Tiwari"'
Publikováno v:
Journal of Chemical Information and Modeling. 60:2570-2580
Cryo-electron microscopy (cryo-EM) single-particle analysis has come a long way in achieving atomic-level resolution when imaging biomolecules. To obtain the best possible three-dimensional (3D) structure in cryo-EM, many parameters have to be carefu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba1af2b7a6dd8ea56bcc1b408bcc500b
https://doi.org/10.1021/acs.jcim.9b01107
https://doi.org/10.1021/acs.jcim.9b01107
Publikováno v:
Journal of chemical information and modeling. 61(8)
X-ray free-electron laser (XFEL) scattering promises to probe single biomolecular complexes without crystallization, enabling the study of biomolecular structures under near-physiological conditions at room temperature. However, such structural deter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0143fe667b68c76bd00547a79d28899e
https://pubmed.ncbi.nlm.nih.gov/34357759
https://pubmed.ncbi.nlm.nih.gov/34357759
Publikováno v:
BMC Bioinformatics, Vol 19, Iss 1, Pp 1-14 (2018)
BMC Bioinformatics
BMC Bioinformatics
Background Advancements in biophysical experimental techniques have pushed the limits in terms of the types of phenomena that can be characterized, the amount of data that can be produced and the resolution at which we can visualize them. Single part
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa30e669a477f0ea62488ffb944e3ee5
http://link.springer.com/article/10.1186/s12859-018-2358-0
http://link.springer.com/article/10.1186/s12859-018-2358-0
Publikováno v:
Journal of molecular biology. 432(9)
The structural and dynamical characterization of biomolecules holds central importance in the endeavor to understand the molecular mechanisms regulating living systems. However, owing to the inherent heterogeneity of biomolecular interactions within
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e63e51c4df9d713e3002e8bdd3077e20
https://pubmed.ncbi.nlm.nih.gov/32061933
https://pubmed.ncbi.nlm.nih.gov/32061933
Publikováno v:
Biochimica et Biophysica Acta-General Subjects
Background: Elastic network models (ENMs) are based on the simple idea that a protein can be described as a set of particles connected by springs, which can then be used to describe its intrinsic flexibility using, for example, normal mode analysis.
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https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10da1ff21bf573fd0f0666ab75b97e51
Publikováno v:
Current opinion in structural biology. 50
The intrinsic dynamics of proteins has been suggested to be the most conserved compared to its sequence or structure. As such, the contributing factors to the conservation of dynamics have yet to be determined definitively. Some have suggested that f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e750107ae3ce0fce434566c28fb1fa4
https://pubmed.ncbi.nlm.nih.gov/29287233
https://pubmed.ncbi.nlm.nih.gov/29287233
Publikováno v:
PLoS Computational Biology
PLoS Computational Biology, Vol 12, Iss 3, p e1004834 (2016)
PLoS Computational Biology, Vol 12, Iss 3, p e1004834 (2016)
The conservation of the intrinsic dynamics of proteins emerges as we attempt to understand the relationship between sequence, structure and functional conservation. We characterise the conservation of such dynamics in a case where the structure is co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85084647bb9ef6ba56881d3ac784255c
http://europepmc.org/articles/PMC4807811
http://europepmc.org/articles/PMC4807811
Autor:
Yasushi Kondo, Jane Clarke, Tina Perica, Xiuwei Zhang, Annette Steward, Sarah A. Teichmann, Sandhya Premnath Tiwari, Katherine R. Kemplen, Nathalie Reuter, Stephen H. McLaughlin
Publikováno v:
Science
Introduction Evolution and design of protein complexes are frequently viewed through the lens of amino acid mutations at protein interfaces, but we showed previously that residues distant from interfaces are also commonly involved in the evolution of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7797c99d360d60eb5e5090d08e429b7c
https://www.repository.cam.ac.uk/handle/1810/246409
https://www.repository.cam.ac.uk/handle/1810/246409
Autor:
Nathalie Reuter, Yasushi Kondo, Annette Steward, Jane Clarke, Tina Perica, Stephen H. McLaughlin, Sandhya Premnath Tiwari, Sarah A. Teichmann
Publikováno v:
Biophysical Journal. 106(2)
Oligomerisation is essential for the function of some proteins. The PyrR family of proteins are involved in pyrimidine operon attenuation. They are regulated by the presence of certain nucleotides such as guanosine monophosphate (GMP), which stabilis
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13d89ac7bb2cc96b59198c79b95a7599
Publikováno v:
Biophysical Journal. 104(2):227a-228a
The eight-fold beta/alpha barrel-like fold, first seen in triose-phosphate isomerase (TIM), is a common and versatile fold for proteins. Proteins in this classification have diverse enzymatic functions spanning five of six Enzyme Commission classes.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::601944d0c3b87bb072e02e7719b3c750