Related ArticlesStructural and orientational constraints of bacteriorhodopsin in purple membranes determined by oriented-sample solid-state NMR spectroscopy.
J Struct Biol. 2005 Jan;149(1):7-16
Authors: Kamihira M, Vosegaard T, Mason AJ, Straus SK, Nielsen NC, Watts A
We report for the first time, oriented-sample solid-state NMR experiments, specifically polarization inversion spin exchange at the magic angle (PISEMA) and 1H-15N heteronuclear chemical shift correlation (HETCOR), applied to an integral seven-transmembrane protein, bacteriorhodopsin (bR), in natural membranes. The spectra of [15N]Met-bR revealed clearly distinguishable signals from the helical and loop regions. By deconvolution of the helix resonances, it was possible to establish constraints for some helix tilt angles. It was estimated that the extracellular section of helix B has a tilt of less than 5 degrees from the membrane normal, while the tilt of helix A was estimated to be 18-22 degrees , both of which are in agreement with most crystal structures. Comparison of the experimental PISEMA spectrum with simulated spectra based on crystal structures showed that PISEMA and HETCOR experiments are extremely sensitive to the polytopic protein structure, and the solid-state NMR spectra for membrane-embedded bR matched most favorably with the recent 1FBB electron crystallography structure. These results suggest that this approach has the potential to yield structural and orientational constraints for large integral polytopic proteins whilst intercalated and functionally competent in a natural membrane.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State Magic-Angle-Spinning NMR
Riqiang Fu, Xingsheng Wang, Conggang Li, Adriana N. Santiago-Miranda, Gary J. Pielak and Fang Tian
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja204062v/aop/images/medium/ja-2011-04062v_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja204062v
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/BuOPwKpaHdw
nmrlearner
Journal club
0
07-27-2011 11:24 AM
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
In Situ Structural Characterization of a Recombinant Protein in Native Escherichia coli Membranes with Solid-State MAS NMR.
J Am Chem Soc. 2011 Jul 21;
Authors: Fu R, Wang X, Li C, Santiago-Miranda AN, Pielak GJ, Tian F
The feasibility of using solid state MAS NMR for in situ structural characterization of the LR11 (sorLA) transmembrane domain in native Escherichia coli (E. coli) membranes is presented. LR11 interacts with...
nmrlearner
Journal club
0
07-23-2011 08:54 AM
[NMR paper] Solid-state NMR yields structural constraints on the V3 loop from HIV-1 Gp120 bound t
Solid-state NMR yields structural constraints on the V3 loop from HIV-1 Gp120 bound to the 447-52D antibody Fv fragment.
Related Articles Solid-state NMR yields structural constraints on the V3 loop from HIV-1 Gp120 bound to the 447-52D antibody Fv fragment.
J Am Chem Soc. 2004 Apr 21;126(15):4979-90
Authors: Sharpe S, Kessler N, Anglister JA, Yau WM, Tycko R
Solid-state NMR measurements were performed on the complex of an 18-residue peptide derived from the V3 loop sequence of the gp120 envelope glycoprotein of the HIV-1 MN strain with Fv...
nmrlearner
Journal club
0
11-24-2010 09:51 PM
[NMR paper] Structural and orientational information of the membrane embedded M13 coat protein by
Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy.
Related Articles Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy.
Biochim Biophys Acta. 2000 Jan 15;1463(1):151-61
Authors: Glaubitz C, Gröbner G, Watts A
Oriented and unoriented M13 coat protein, incorporated into dimyristoyl phosphatidylcholine bilayers, has been studied by (13)C-magic angle spinning nuclear magnetic resonance (MAS NMR) spectroscopy. Rotational...
nmrlearner
Journal club
0
11-18-2010 09:15 PM
[NMR paper] Protein structural analysis from solid-state NMR-derived orientational constraints.
Protein structural analysis from solid-state NMR-derived orientational constraints.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Protein structural analysis from solid-state NMR-derived orientational constraints.
Biophys J. 1997 May;72(5):2342-8
Authors: Quine JR, Brenneman MT, Cross TA
High-resolution orientational constraints from solid-state NMR...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[NMR paper] Protein structural analysis from solid-state NMR-derived orientational constraints.
Protein structural analysis from solid-state NMR-derived orientational constraints.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-cellhub.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Protein structural analysis from solid-state NMR-derived orientational constraints.
Biophys J. 1997 May;72(5):2342-8
Authors: Quine JR, Brenneman MT, Cross TA
High-resolution orientational constraints from solid-state NMR...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[NMR paper] Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C
Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Related Articles Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Biochemistry. 1994 May 31;33(21):6433-41
Authors: Pochapsky TC, Ratnaswamy G, Patera A
Putidaredoxin (Pdx) is a 106-residue Fe2S2 ferredoxin which acts as the physiological reductant and effector of cytochrome P-450cam. Pdx has two accessible oxidation states, Fe+3-Fe+3 (oxidized) and...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C
Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Related Articles Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
Biochemistry. 1994 May 31;33(21):6433-41
Authors: Pochapsky TC, Ratnaswamy G, Patera A
Putidaredoxin (Pdx) is a 106-residue Fe2S2 ferredoxin which acts as the physiological reductant and effector of cytochrome P-450cam. Pdx has two accessible oxidation states, Fe+3-Fe+3 (oxidized) and...
Structural and orientational constraints of bacteriorhodopsin in purple membranes det
Linear Mode
