Nmr characterization of self-association domains promoted by interactions with lc8 hub protein
NMR CHARACTERIZATION OF SELF-ASSOCIATION DOMAINS PROMOTED BY INTERACTIONS WITH LC8 HUB PROTEIN
Publication date: February 2014
Source:Computational and Structural Biotechnology Journal, Volume 9, Issue 14</br>
Author(s): Elisar Barbar , Afua Nyarko</br>
Most proteins in interaction networks have a small number of partners, while a few, called hubs, participate in a large number of interactions and play a central role in cell homeostasis. One highly conserved hub is a protein called LC8 that was originally identified as an essential component of the multi-subunit...
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[NMR paper] NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.
NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.
Related Articles NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.
Comput Struct Biotechnol J. 2014;9:e201402003
Authors: Barbar E, Nyarko A
Abstract
Most proteins in interaction networks have a small number of partners, while a few, called hubs, participate in a large number of interactions and play a central role in cell homeostasis. One highly conserved hub is a protein called LC8...
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja410287s/aop/images/medium/ja-2013-10287s_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja410287s
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http://feeds.feedburner.com/~r/acs/jacsat/~4/ZN4MowZBRDs
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http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206516u/aop/images/medium/ja-2011-06516u_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206516u
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Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Combination of NMR spectroscopy and X-ray crystallography offers unique advantages for elucidation of the structural basis of protein complex assembly.
Sci China Life Sci. 2011 Feb;54(2):101-11
Authors: Feng W, Pan L, Zhang M
NMR spectroscopy and X-ray crystallography are two premium methods for determining the atomic structures of macro-biomolecular complexes. Each method has unique strengths and...
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02-15-2011 07:17 PM
[NMR paper] Amphipathic helical behavior of the third repeat fragment in the tau microtubule-bind
Amphipathic helical behavior of the third repeat fragment in the tau microtubule-binding domain, studied by (1)H NMR spectroscopy.
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The third repeat fragment (3MBD, 31 residues) in the four-repeat microtubule-binding domain of water-soluble tau protein has been considered to...
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[NMR paper] 19F and 31P NMR spectroscopy of G protein alpha subunits. Mechanism of activation by
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J Biol Chem. 1991 Feb 25;266(6):3396-401
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19F and 31P NMR spectroscopy was used to study the mechanism of activation of the alpha subunits of guanine nucleotide-binding regulatory proteins (G proteins) by Al3+, Mg2+, and F-. 19F NMR spectra of solutions containing Al3+,...
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Biochim Biophys Acta. 1990 Nov 15;1041(2):186-94
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The...
Mechanism of Tau-Promoted Microtubule Assembly AsProbed by NMR Spectroscopy
Linear Mode
