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pro vyhledávání: '"Leanna R. McDonald"'
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
The computational prediction of protein allostery can guide experimental studies of protein function and cellular activity. Here, the authors develop a network-based method to detect allosteric coupling within proteins solely based on their structure
Externí odkaz:
https://doaj.org/article/02fe4867530c4119b85459cc38ba7e72
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Nature Communications
Nature Communications
Allostery in proteins influences various biological processes such as regulation of gene transcription and activities of enzymes and cell signaling. Computational approaches for analysis of allosteric coupling provide inexpensive opportunities to pre
Publikováno v:
Biophysical Journal. 108(2):60a-61a
Protein kinases regulate various important cellular signaling events by catalyzing phosphoryl transfer from ATP to the hydroxyl groups of their substrates. Aberrant protein phosphorylation is linked to fatal diseases including cancer and cardiac dise
Publikováno v:
Journal of molecular biology. 425(13)
It is now widely recognized that dynamics are important to consider for understanding allosteric protein function. However, dynamics occur over a wide range of timescales, and how these different motions relate to one another is not well understood.
Publikováno v:
Structure (London, England : 1993). 20(8)
SummaryThe switch between an inactive and active conformation is an important transition for signaling proteins, yet the mechanisms underlying such switches are not clearly understood. Escherichia coli CheY, a response regulator protein from the two-