[ASAP] Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor
Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor
Matthew T. Eddy, Zhan-Guo Gao, Philip Mannes, Nilkanth Patel, Kenneth A. Jacobson, Vsevolod Katritch, Raymond C. Stevens, Kurt Wüthrich
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.8b03805/20180620/images/medium/ja-2018-03805n_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.8b03805
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA...
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06-21-2018 09:01 AM
[NMR paper] Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor.
Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor.
Extrinsic Tryptophans as NMR Probes of Allosteric Coupling in Membrane Proteins: Application to the A2A Adenosine Receptor.
J Am Chem Soc. 2018 Jun 06;:
Authors: Eddy MT, Gao ZG, Mannes P, Patel N, Jacobson KA, Katritch V, Stevens RC, Wüthrich K
Abstract
Tryptophan indole 15N-1H signals are well separated in nuclear magnetic resonance (NMR) spectra of proteins. Assignment of the indole 15N-1H signals...
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06-07-2018 01:52 PM
[ASAP] Strategy for Stabilization of CutA1 Proteins Due to Ion–Ion Interactions at Temperatures of over 100 °C
Strategy for Stabilization of CutA1 Proteins Due to Ion–Ion Interactions at Temperatures of over 100 °C
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00103/20180418/images/medium/bi-2018-00103y_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00103
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http://feeds.feedburner.com/~r/acs/bichaw/~4/RydMtktKULY
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04-19-2018 01:51 AM
[NMR paper] Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR.
Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR.
Conformational stabilization of the membrane embedded targeting domain of the lysosomal peptide transporter TAPL for solution NMR.
J Biomol NMR. 2013 Sep 7;
Authors: Tumulka F, Roos C, Löhr F, Bock C, Bernhard F, Dötsch V, Abele R
Abstract
The ATP binding cassette transporter TAPL translocates cytosolic peptides into the lumen of lysosomes driven by the hydrolysis of ATP. Functionally, this transporter can be...
Extrinsic stabilization of antiviral ACE2-Fc fusion proteins targeting ... - Nature.com
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