[ASAP] Identifying the Protein Interactions of the Cytosolic Iron–Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets
Identifying the Protein Interactions of the Cytosolic Iron–Sulfur Cluster Targeting Complex Essential for Its Assembly and Recognition of Apo-Targets
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00072/20180409/images/medium/bi-2017-00072x_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00072
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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nmrlearner
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04-10-2018 12:35 AM
Essential Role of the Linker Region in the HigherCatalytic Efficiency of a Bifunctional MsrA–MsrB Fusion Protein
Essential Role of the Linker Region in the HigherCatalytic Efficiency of a Bifunctional MsrA–MsrB Fusion Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00544/20160901/images/medium/bi-2016-005445_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00544
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nmrlearner
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09-01-2016 07:21 PM
[NMR paper] NMR Structure of Integrin ?4 Cytosolic Tail and Its Interactions with Paxillin.
NMR Structure of Integrin ?4 Cytosolic Tail and Its Interactions with Paxillin.
Related Articles NMR Structure of Integrin ?4 Cytosolic Tail and Its Interactions with Paxillin.
PLoS One. 2013;8(1):e55184
Authors: Chua GL, Patra AT, Tan SM, Bhattacharjya S
Abstract
BACKGROUND: Integrins are a group of transmembrane signaling proteins that are important in biological processes such as cell adhesion, proliferation and migration. Integrins are ?/? hetero-dimers and there are 24 different integrins formed by specific combinations of 18 ? and 8...
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02-06-2013 10:18 PM
[NMR paper] Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.
J Biomol NMR. 2013 Jan 24;
Authors: Emami S, Fan Y, Munro R, Ladizhansky V, Brown LS
Abstract
One of the biggest challenges in solid-state NMR studies of membrane proteins is to obtain a...
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02-03-2013 10:19 AM
NMR techniques in drug delivery: Application to zein protein complexes
NMR techniques in drug delivery: Application to zein protein complexes
15 December 2012
Publication year: 2012
Source:International Journal of Pharmaceutics, Volume 439, Issues 1–2</br>
</br>
Zein is a protein containing a large amount of nonpolar amino acids, which has shown the ability to form aggregates and entrap solutes, such as drugs and amino acids. NMR techniques were used to detect binding interactions and measure affinity between zein and three different drugs: tetracycline, amoxicillin and indomethacin. The release study of zein microparticle formulations...
nmrlearner
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02-03-2013 10:13 AM
[KPWU blog] pynmr ? an excellent PyMol?s NMR extension
pynmr ? an excellent PyMol?s NMR extension
When I installed PyMol on my iMac using Fink, I found there are some plugins installed already. One of the famous plugin is PDB loader, I believe every one loves it a lot. A new one (at least it’s new to me) is NMR extension written by a Canadian group. Thank you! I’m lovin it http://stats.wordpress.com/b.gif?host=kpwu.wordpress.com&blog=76132&post=301&subd=kpwu&ref=&feed=1
Go to KPWU blog to read complete post.
nmrlearner
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04-02-2011 09:44 AM
[NMR paper] Improved efficiency of protein structure calculations from NMR data using the program
Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
Related Articles Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
J Biomol NMR. 1991 Nov;1(4):447-56
Authors: Güntert P, Wüthrich K
A new strategy for NMR structure calculations of proteins with the variable target function method (Braun, W. and Go, N. (1985) J. Mol. Biol., 186, 611) is described, which makes use of...
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08-21-2010 11:12 PM
[NMR paper] Improved efficiency of protein structure calculations from NMR data using the program
Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
Related Articles Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.
J Biomol NMR. 1991 Nov;1(4):447-56
Authors: Güntert P, Wüthrich K
A new strategy for NMR structure calculations of proteins with the variable target function method (Braun, W. and Go, N. (1985) J. Mol. Biol., 186, 611) is described, which makes use of...