Receptor Activity Modifying Proteins Have LimitedEffects on the Class B G Protein-Coupled Receptor Calcitonin Receptor-LikeReceptor Stalk
Receptor Activity Modifying Proteins Have LimitedEffects on the Class B G Protein-Coupled Receptor Calcitonin Receptor-LikeReceptor Stalk
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01180/20180207/images/medium/bi-2017-01180k_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01180
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02-08-2018 04:02 AM
[NMR paper] Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.
Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.
Expression, Functional Characterization, and Solid-State NMR Investigation of the G Protein-Coupled GHS Receptor in Bilayer Membranes.
Sci Rep. 2017 Apr 07;7:46128
Authors: Schrottke S, Kaiser A, Vortmeier G, Els-Heindl S, Worm D, Bosse M, Schmidt P, Scheidt HA, Beck-Sickinger AG, Huster D
Abstract
The expression, functional reconstitution and first NMR characterization of the human growth...
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04-08-2017 10:57 AM
[NMR paper] NMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates.
NMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates.
Related Articles NMR Investigation of Structures of G-Protein Coupled Receptor Folding Intermediates.
J Biol Chem. 2016 Nov 18;:
Authors: Poms M, Ansorge P, Martinez-Gil L, Jurt S, Gottstein D, Fracchiolla KE, Cohen LS, Guentert P, Mingarro I, Naider F, Zerbe O
Abstract
Folding of G-protein coupled receptors (GPCRs) according to the two-stage model (Popot et al., Biochemistry 29(1990), 4031) is postulated to proceed in 2 steps: Partitioning of...
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11-20-2016 09:20 PM
Investigation of the Binding Interaction of FattyAcids with Human G Protein-Coupled Receptor 40 Using a Site-SpecificFluorescence Probe by Flow Cytometry
Investigation of the Binding Interaction of FattyAcids with Human G Protein-Coupled Receptor 40 Using a Site-SpecificFluorescence Probe by Flow Cytometry
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00079/20160317/images/medium/bi-2016-00079r_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00079
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03-18-2016 04:29 AM
NMR as a tool to identify and characterize protein folding intermediates
NMR as a tool to identify and characterize protein folding intermediates
Available online 12 September 2012
Publication year: 2012
Source:Archives of Biochemistry and Biophysics</br>
</br>
NMR spectroscopy is one of the few biophysical methods that can provide atomic-level insight into the conformation of partially folded states and/or intermediates present along the protein folding pathway. Such studies are important not only within the context of the protein folding problem, but also to push forward the technique, due to the challenging nature of the systems studied....
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02-03-2013 10:13 AM
The Chemoselective Reactions of Tyrosine-Containing G-Protein-Coupled Receptor Peptides with [Cp*Rh(H2O)3](OTf)2, Including 2D NMR Structures and the Biological Consequences
The Chemoselective Reactions of Tyrosine-Containing G-Protein-Coupled Receptor Peptides with (OTf)2, Including 2D NMR Structures and the Biological Consequences
H. Bauke Albada, Florian Wieberneit, Ingrid Dijkgraaf, Jessica H. Harvey, Jennifer L. Whistler, Raphael Stoll, Nils Metzler-Nolte and Richard H. Fish
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja303010k/aop/images/medium/ja-2012-03010k_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja303010k
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06-16-2012 06:01 AM
[NMR paper] Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide ex
Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange-two-dimensional NMR spectroscopy.
Related Articles Investigation of ribonuclease T1 folding intermediates by hydrogen-deuterium amide exchange-two-dimensional NMR spectroscopy.
Biochemistry. 1993 Jun 22;32(24):6152-6
Authors: Mullins LS, Pace CN, Raushel FM
The rate of hydrogen bond formation at individual amino acid residues in ribonuclease T1 (RNase T1) has been investigated by the hydrogen-deuterium exchange-2D NMR (HDEx-2D NMR) technique (Udgaonkar...