Related ArticlesDynamic aspect of bacteriorhodopsin as a typical membrane protein as revealed by site-directed solid-state 13C NMR.
Solid State Nucl Magn Reson. 2004 Jan;25(1-3):5-14
Authors: Saitô H, Yamaguchi S, Okuda H, Shiraishi A, Tuzi S
We demonstrate here a general feature of dynamic aspect of membrane proteins as revealed by site-directed 13C NMR studies on bacteriorhodopsin (bR) as a typical membrane protein and a variety of mutants at ambient temperature. 13C NMR signals of [3-13C]Ala- or [1-13C]Val-labeled proteins were assigned regio-specifically with reference to the data of the conformation-dependent 13C chemical shifts from model polypeptides, followed by site-specific assignment based on site-directed mutants. Revealed picture of membrane protein at ambient temperature is not static in contrast to anticipation from crystalline structures but flexible enough to undergo a variety of local fluctuations with frequencies from 10(2) to 10(8)Hz, as pointed out already. This picture was further refined by taking into account of residue-specific dynamics of interfacial domains between the surface and inner part of the transmembrane helices and conformational fluctuation induced by the presence of a kinked structure. The residue-specific dynamics of the former was revealed by observation of broadened or suppressed peaks from the interfacial domains caused by acquisition of internal fluctuation motions interfered with frequencies of proton decoupling or magic angle spinning. The presence of such suppressed peaks due to molecular fluctuations in the interfacial domains was further confirmed by insensitivity of the peak-intensities from the interfacial domains in spite of the presence of accelerated relaxation rate to nearby residues from surface bound Mn2+ ion. Further, conformational change of the transmembrane alpha-helix F due to a plausible kinked structure at Pro 186 was confirmed in view of specific displacements of Ala 184 and Val 187 13C NMR peaks from chemically synthesized [3-13C]Ala(184)-, [1-13C]Val(187)-labeled wild type and P186L mutant of transmembrane fragment F(164-194) incorporated into lipid bilayer. It is emphasized that the observed displacement of [3-13C]-labeled Ala 184 peak at 17.4 ppm in the presence of kinked structure in this model peptide is consistent with that of intact protein at 17.27 ppm.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Dynamic structure of bombolitin II bound to lipid bilayers as revealed by solid-state NMR and molecular-dynamics simulation.
Biophys J. 2010 Nov 17;99(10):3282-9
Authors: Toraya S, Javkhlantugs N, Mishima D, Nishimura K, Ueda K, Naito A
Bombolitin II (BLT2) is one of the hemolytic heptadecapeptides originally isolated from the venom of a bumblebee. Structure and orientation of BLT2 bound to...
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[NMR paper] 'Boomerang'-like insertion of a fusogenic peptide in a lipid membrane revealed by sol
'Boomerang'-like insertion of a fusogenic peptide in a lipid membrane revealed by solid-state 19F NMR.
Related Articles 'Boomerang'-like insertion of a fusogenic peptide in a lipid membrane revealed by solid-state 19F NMR.
Magn Reson Chem. 2004 Feb;42(2):195-203
Authors: Afonin S, Dürr UH, Glaser RW, Ulrich AS
Solid state (19)F NMR revealed the conformation and alignment of the fusogenic peptide sequence B18 from the sea urchin fertilization protein bindin embedded in flat phospholipid bilayers. Single (19)F labels were introduced into nine...
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11-24-2010 09:25 PM
[NMR paper] Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
Related Articles Conformation and backbone dynamics of bacteriorhodopsin revealed by (13)C-NMR.
Biochim Biophys Acta. 2000 Aug 30;1460(1):39-48
Authors: Saitô H, Tuzi S, Yamaguchi S, Tanio M, Naito A
It is demonstrated here how the secondary structure and dynamics of transmembrane helices, as well as surface residues, such as interhelical loops and N- or C-terminus of bacteriorhodopsin (bR) in purple membrane, can be determined at ambient temperature based on very...
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11-19-2010 08:29 PM
[NMR paper] The dynamic properties of the M121H azurin metal site as studied by NMR of the parama
The dynamic properties of the M121H azurin metal site as studied by NMR of the paramagnetic Cu(II) and Co(II) metalloderivatives.
Related Articles The dynamic properties of the M121H azurin metal site as studied by NMR of the paramagnetic Cu(II) and Co(II) metalloderivatives.
J Biol Chem. 1998 Jan 2;273(1):177-85
Authors: Salgado J, Kroes SJ, Berg A, Moratal JM, Canters GW
The M121H azurin mutant in solution presents various species in equilibrium that can be detected and studied by 1H NMR of the Cu(II) and Co(II) paramagnetic...
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11-17-2010 11:06 PM
[NMR paper] Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NM
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
Biochemistry. 1997 Jan 28;36(4):699-710
Authors: Zhou H, Dahlquist FW
Bacterial chemotaxis involves autophosphorylation of a histidine kinase and transfer of the phosphoryl group to response regulators to control flagellar rotation and receptor adaptation. The...
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08-22-2010 03:31 PM
[NMR paper] Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NM
Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Phosphotransfer site of the chemotaxis-specific protein kinase CheA as revealed by NMR.
Biochemistry. 1997 Jan 28;36(4):699-710
Authors: Zhou H, Dahlquist FW
Bacterial chemotaxis involves autophosphorylation of a histidine kinase and transfer of the phosphoryl group to response regulators to control flagellar rotation and receptor adaptation. The...
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08-22-2010 03:03 PM
[NMR paper] NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies
NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates.
Biochemistry. 1996 Jul 30;35(30):9637-46
Authors: Scheuring J, Fischer M, Cushman M, Lee J, Bacher A,...
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[NMR paper] Rotational resonance NMR study of the active site structure in bacteriorhodopsin: con
Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage.
Related Articles Rotational resonance NMR study of the active site structure in bacteriorhodopsin: conformation of the Schiff base linkage.
Biochemistry. 1992 Sep 1;31(34):7931-8
Authors: Thompson LK, McDermott AE, Raap J, van der Wielen CM, Lugtenburg J, Herzfeld J, Griffin RG
Rotational resonance, a new solid-state NMR technique for determining internuclear distances, is used to measure a distance in the active site of...