Related ArticlesCharacterization of the Simultaneous Decay Kinetics of Metarhodopsin States II and III in Rhodopsin by Solution-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2014 Feb 6;
Authors: Stehle J, Silvers R, Werner K, Chatterjee D, Gande S, Scholz F, Dutta A, Wachtveitl J, Klein-Seetharaman J, Schwalbe H
Abstract
The mammalian visual dim-light photoreceptor rhodopsin is considered a prototype G protein-coupled receptor. Here, we characterize the kinetics of its light-activation process. Milligram quantities of ?,?-(15) N-labeled tryptophan rhodopsin were produced in stably transfected HEK293 cells. Assignment of the chemical shifts of the indole signals was achieved by generating the single-point-tryptophan to phenylalanine mutants, and the kinetics of each of the five tryptophan residues were recorded. We find kinetic partitioning in rhodopsin decay, including three half-lives, that reveal two parallel processes subsequent to rhodopsin activation that are related to the photocycle. The meta II and meta III states emerge in parallel with a relative ratio of about 3:1. Transient formation of the meta III state was confirmed by flash photolysis experiments. From analysis of the site-resolved kinetic data we propose the involvement of the E2 -loop in the formation of the meta III state.
PMID: 24505031 [PubMed - as supplied by publisher]
Expression, Purification, and Solid-State NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in Two Electronic Spin States
Expression, Purification, and Solid-State NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in Two Electronic Spin States
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi401020t/aop/images/medium/bi-2013-01020t_0007.gif
Biochemistry
DOI: 10.1021/bi401020t
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[NMR paper] Expression, Purification and Solid-state NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in two Electronic Spin States.
Expression, Purification and Solid-state NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in two Electronic Spin States.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Expression, Purification and Solid-state NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in two Electronic Spin States.
Biochemistry. 2013 Sep 13;
Authors: Varghese S, Yang F, Pacheco V, Wrede K, Medvedev A, Ogata H, Knipp M, Heise H
Abstract
The...
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09-17-2013 11:36 PM
[NMR paper] Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.
Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.
J Biomol NMR. 2013 Aug 24;
Authors: Bernard D, Bédard M, Bilodeau J, Lavigne P
Abstract
Myc-interacting zinc finger protein-1 (Miz-1) is a BTB/POZ transcription factor that activates the...
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[NMR paper] Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.
Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.
Biochim Biophys Acta. 2013 Jul 16;
Authors: Létourneau D, Lorin A, Lefebvre A, Cabana J, Lavigne P, Lehoux JG
Abstract
STARD5 is a member of the STARD4 sub-family...
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Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1148-53
Authors: Buchko GW, Hewitt SN, Napuli AJ, Van Voorhis WC, Myler PJ
Abstract
Owing to the evolution of multi-drug-resistant and extremely drug-resistant Mycobacterium tuberculosis strains,...
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Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.
Measurement of protein unfolding/refolding kinetics and structural characterization of hidden intermediates by NMR relaxation dispersion.
Proc Natl Acad Sci U S A. 2011 May 11;
Authors: Meinhold DW, Wright PE
Detailed understanding of protein function and malfunction hinges on the ability to characterize transiently populated states and the transitions between them. Here, we use (15)N, , and (13)CO NMR R(2)...
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05-13-2011 02:40 PM
[NMR paper] Deuterium NMR structure of retinal in the ground state of rhodopsin.
Deuterium NMR structure of retinal in the ground state of rhodopsin.
Related Articles Deuterium NMR structure of retinal in the ground state of rhodopsin.
Biochemistry. 2004 Oct 12;43(40):12819-28
Authors: Salgado GF, Struts AV, Tanaka K, Fujioka N, Nakanishi K, Brown MF
The conformation of retinal bound to the G protein-coupled receptor rhodopsin is intimately linked to its photochemistry, which initiates the visual process. Site-directed deuterium ((2)H) NMR spectroscopy was used to investigate the structure of retinal within the binding...
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[NMR paper] Retinylidene ligand structure in bovine rhodopsin, metarhodopsin-I, and 10-methylrhod
Retinylidene ligand structure in bovine rhodopsin, metarhodopsin-I, and 10-methylrhodopsin from internuclear distance measurements using 13C-labeling and 1-D rotational resonance MAS NMR.
Related Articles Retinylidene ligand structure in bovine rhodopsin, metarhodopsin-I, and 10-methylrhodopsin from internuclear distance measurements using 13C-labeling and 1-D rotational resonance MAS NMR.
Biochemistry. 1999 Aug 31;38(35):11316-24
Authors: Verdegem PJ, Bovee-Geurts PH, de Grip WJ, Lugtenburg J, de Groot HJ
Rhodopsin is the G-protein coupled...
Characterization of the Simultaneous Decay Kinetics of Metarhodopsin States II and III in Rhodopsin by Solution-State NMR Spectroscopy.
Linear Mode
