NMR imprint of intersubunit communication [Biophysics and Computational Biology]
NMR imprint of intersubunit communication
Falk, B. T., Sapienza, P. J., Lee, A. L....
Date: 2016-08-23
Allosteric communication is critical for protein function and cellular homeostasis, and it can be exploited as a strategy for drug design. However, unlike many protein–ligand interactions, the structural basis for the long-range communication that underlies allostery is not well understood. This lack of understanding is most evident in the case... Read More
PNAS:
Number: 34
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StructuralPolymorphism of Alzheimer’s ?-AmyloidFibrils as Controlled by an E22 Switch: A Solid-State NMR Study
StructuralPolymorphism of Alzheimer’s ?-AmyloidFibrils as Controlled by an E22 Switch: A Solid-State NMR Study
Matthew R. Elkins, Tuo Wang, Mimi Nick, Hyunil Jo, Thomas Lemmin, Stanley B. Prusiner, William F. DeGrado, Jan Sto?hr and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b03715/20160728/images/medium/ja-2016-03715q_0011.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b03715
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http://feeds.feedburner.com/~r/acs/jacsat/~4/cM2mgHkI5JQ
[NMR paper] Intra- and inter-molecular interactions of human galectin-3: assessment by full-assignment-based NMR.
Intra- and inter-molecular interactions of human galectin-3: assessment by full-assignment-based NMR.
Related Articles Intra- and inter-molecular interactions of human galectin-3: assessment by full-assignment-based NMR.
Glycobiology. 2016 Feb 23;
Authors: Ippel H, Miller MC, Vértesy S, Zhang Y, Cańada FJ, Suylen D, Umemoto K, Romanň C, Hackeng T, Tai G, Leffler H, Kopitz J, André S, Kübler D, Jiménez-Barbero J, Oscarson S, Gabius HJ, Mayo KH
Abstract
Galectin-3 is an adhesion/growth-regulatory protein with a modular design...
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HighResolution Structural Characterization of A?42 AmyloidFibrils by Magic Angle Spinning NMR
HighResolution Structural Characterization of A?42 AmyloidFibrils by Magic Angle Spinning NMR
Michael T. Colvin, Robert Silvers, Birgitta Frohm, Yongchao Su, Sara Linse and Robert G. Griffin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.5b03997/20150604/images/medium/ja-2015-03997u_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.5b03997
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http://feeds.feedburner.com/~r/acs/jacsat/~4/KbGlyz-E4EI
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Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Biochim Biophys Acta. 2011 Jan;1808(1):498-507
Authors: Mishra VK, Palgunachari MN, Hudson JS, Shin R, Keenum TD, Krishna NR, Anantharamaiah GM
The surprising observation that a 10-residue class G(?) peptide from apolipoprotein J, apoJ, possesses...
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[NMR paper] Solution-state NMR investigation of DNA binding interactions in Escherichia coli form
Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface.
Related Articles Solution-state NMR investigation of DNA binding interactions in Escherichia coli formamidopyrimidine-DNA glycosylase (Fpg): a dynamic description of the DNA/protein interface.
DNA Repair (Amst). 2005 Mar 2;4(3):327-39
Authors: Buchko GW, McAteer K, Wallace SS, Kennedy MA
Formamidopyrimidine-DNA glycosylase (Fpg) is a base excision repair (BER) protein...
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[NMR paper] A NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat
A NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat protein with lipids, which mimic the Escherichia coli inner membrane.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles A NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat protein with lipids, which mimic the Escherichia coli inner membrane.
Biochim Biophys Acta. 1991 Jul 1;1066(1):102-8
Authors: Sanders JC, Poile TW, Spruijt RB, Van Nuland NA, Watts A, Hemminga MA
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