New interaction mechanism of proteins discovered | EurekAlert ... - EurekAlert (press release)
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New interaction mechanism of proteins discovered | EurekAlert ...
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UZH researchers have discovered a previously unknown way in which proteins interact with one another and cells organize themselves. This new mechanism involves two fully unstructured proteins forming an ultra-high-affinity complex due to their opposite ...
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02-22-2018 02:13 AM
[NMR paper] Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.
Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.
Sci Rep. 2017 Nov 28;7(1):16462
Authors: Minato Y, Ueda T, Machiyama A, Iwaï H, Shimada I
Abstract
Bacteria utilize thermotaxis signal transduction proteins, including CheA, and CheY, to switch the direction of the cell...
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12-01-2017 09:24 PM
A Noncanonical Binding Site in the EVH1 Domain ofVasodilator-Stimulated Phosphoprotein Regulates Its Interactions withthe Proline Rich Region of Zyxin
A Noncanonical Binding Site in the EVH1 Domain ofVasodilator-Stimulated Phosphoprotein Regulates Its Interactions withthe Proline Rich Region of Zyxin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00618/20170823/images/medium/bi-2017-006182_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00618
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/eYP-qgKgrgs
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08-24-2017 08:38 AM
Study shows how mutations disrupt ALS-linked protein | EurekAlert ... - EurekAlert (press release)
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Study shows how mutations disrupt ALS-linked protein | EurekAlert ...
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Structural biologists provide a new explanation for how ALS-associated genetic flaws interfere with the proper function and behavior of the protein TDP-43.
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Study shows how mutations disrupt ALS-linked protein | EurekAlert ... - EurekAlert (press release)
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08-19-2016 04:05 AM
Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
Insight into interactions of the von-Willebrand-factor-A-like domain 2 with the FNIII-like domain 9 of collagen VII by NMR and SPR.
FEBS Lett. 2011 May 9;
Authors: Leineweber S, Schönig S, Seeger K
Type VII collagen as component of anchoring fibrils plays an important role in skin architecture, however, no detailed structural information is available. Here, we describe the recombinant expression, isotope labeling, and...