[NMR paper] Signaling-Related Mobility Changes in Bacterial Chemotaxis Receptors Revealed by Solid-State NMR.
Signaling-Related Mobility Changes in Bacterial Chemotaxis Receptors Revealed by Solid-State NMR.
Signaling-Related Mobility Changes in Bacterial Chemotaxis Receptors Revealed by Solid-State NMR.
J Phys Chem B. 2017 Aug 17;:
Authors: Kashefi M, Thompson LK
Abstract
Bacteria employ remarkable membrane-bound nanoarrays to sense their environment and direct their swimming. Arrays consist of chemotaxis receptor trimers of dimers that are bridged at their membrane-distal tips by rings of two cytoplasmic proteins, a kinase CheA and a...
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08-18-2017 04:59 PM
Posttranslational Modification of Heme b in a Bacterial Peroxidase: The Role of Heme to Protein Ester Bondsin Ligand Binding and Catalysis
Posttranslational Modification of Heme b in a Bacterial Peroxidase: The Role of Heme to Protein Ester Bondsin Ligand Binding and Catalysis
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00632/20170815/images/medium/bi-2017-00632n_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00632
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08-17-2017 12:56 AM
Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human ?C-Crystallin: Role of the Dipole Moment in Protein Solubility
Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human ?C-Crystallin: Role of the Dipole Moment in Protein Solubility
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00359/20160521/images/medium/bi-2016-00359c_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00359
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05-23-2016 10:51 PM
[NMR paper] NMR structure of a major lens protein, Human ?C-Crystallin: Role of dipole moment in protein solubility.
NMR structure of a major lens protein, Human ?C-Crystallin: Role of dipole moment in protein solubility.
Related Articles NMR structure of a major lens protein, Human ?C-Crystallin: Role of dipole moment in protein solubility.
Biochemistry. 2016 May 17;
Authors: Dixit K, Pande A, Pande J, Sarma SP
Abstract
A hallmark of the crystallin proteins is their exceptionally high solubility, which is vital for maintaining the high refractive index of the eye lens. Human ?C-crystallin is a major ?-crystallin whose mutant forms are...
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05-18-2016 09:53 PM
Scientists Observe Structure of Protein That Plays Major Role in Huntington's Disease, Opening Door to Finding Cause ... - Huntington's Disease News
Scientists Observe Structure of Protein That Plays Major Role in Huntington's Disease, Opening Door to Finding Cause ... - Huntington's Disease News
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Huntington's Disease News
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Scientists Observe Structure of Protein That Plays Major Role in Huntington's Disease, Opening Door to Finding Cause ...
Huntington's Disease News
Leibniz-Institut für Molekulare Pharmakologie (FMP) researchers used a combination of nuclear magnetic...
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02-10-2016 09:28 PM
[NMR images] cspa is the major cold shock protein of the bacterial
http://www-nmr.cabm.rutgers.edu/photogallery/proteins/gif/3MEF-v3b.jpg
20/03/2014 12:45:23 PM GMT
cspa is the major cold shock protein of the bacterial
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NMR pictures
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03-20-2014 12:44 PM
[NMR paper] NMR study suggests a major role for Arg111 in maintaining the structure and dynamical
NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Related Articles NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein.
Biochemistry. 1998 Sep 15;37(37):13021-32
Authors: Wang L, Yan H
The solution structure of a site-directed mutant of type-II human cellular retinoic acid binding protein (CRABPII) with Arg111 replaced by methionine (R111M)...