Related ArticlesDynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramicidin.
Biophys J. 1994 May;66(5):1429-40
Authors: Prosser RS, Davis JH
Solid state deuterium (2H) NMR inversion-recovery and Jeener-Broekaert relaxation experiments were performed on oriented multilamellar dispersions consisting of 1,2-dilauroyl-sn-glycero-3-phosphatidylcholine and 2H exchange-labeled gramicidin D, at a lipid to protein molar ratio (L/P) of 15:1, in order to study the dynamics of the channel conformation of the peptide in a liquid crystalline phase. Our dynamic model for the whole body motions of the peptide includes diffusion of the peptide around its helix axis and a wobbling diffusion around a second axis perpendicular to the local bilayer normal in a simple Maier-Saupe mean field potential. This anisotropic diffusion is characterized by the correlation times, tau R parallel and tau R perpendicular. Aligning the bilayer normal perpendicular to the magnetic field and graphing the relaxation rate, 1/T1Z, as a function of (1-S2N-2H), where S2N-2H represents the orientational order parameter, wer were able to estimate the correlation time, tau R parallel, for rotational diffusion. Although in the quadrupolar splitting, which varies as (3 cos2 theta D-1), has in general two possible solutions to theta D in the range 0 < or = theta D < or = 90 degrees, the 1/T1Z vs. (1-S2N-2H) curve can be used to determine a single value of theta D in this range. Thus, the 1/T1Z vs. (1-S2N-2H) profile can be used both to define the axial diffusion rate and to remove potential structural ambiguities in the splittings. The T1Z anisotropy permits us to solve for the two correlation times (tau R parallel = 6.8 x 10(-9) s and tau R perpendicular = 6 x 10(-6) s). The simulated parameters were corroborated by a Jeener-Broekaert experiment where the bilayer normal was parallel to the principal magnetic field. At this orientation the ratio, J2(2 omega 0)/J1(omega 0) was obtained in order to estimate the strength of the restoring potential in a model-independent fashion. This measurement yields the rms angle, 1/2 (= 16 +/- 2 degrees at 34 degrees C), formed by the peptide helix axis and the average bilayer normal.
Solution NMR study of integral membrane proteins.
Solution NMR study of integral membrane proteins.
Solution NMR study of integral membrane proteins.
Curr Opin Chem Biol. 2011 Jun 18;
Authors: Kang C, Li Q
Signals between a cell and its environment are often transmitted through membrane proteins; therefore, many membrane proteins, including G protein-coupled receptors (GPCRs) and ion channels, are important drug targets. Structural information about membrane proteins remains limited owing to challenges in protein expression, purification and the selection of membrane-mimicking systems that will...
nmrlearner
Journal club
0
06-21-2011 01:50 PM
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
Deuterium Magic Angle Spinning NMR Used to Study the Dynamics of Peptides Adsorbed onto Polystyrene and Functionalized Polystyrene Surfaces.
J Phys Chem B. 2011 Jun 8;
Authors: Breen NF, Li K, Olsen GL, Drobny GP
LK?14 is a 14 amino acid peptide which displays a periodic alternation of leucine and lysine amino acids. This "hydrophobic periodicity" has been found to result in an ?-helical secondary structure...
nmrlearner
Journal club
0
06-10-2011 11:52 AM
[NMR paper] How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Related Articles How to prepare membrane proteins for solid-state NMR: A case study on the alpha-helical integral membrane protein diacylglycerol kinase from E. coli.
Chembiochem. 2005 Sep;6(9):1693-700
Authors: Lorch M, Faham S, Kaiser C, Weber I, Mason AJ, Bowie JU, Glaubitz C
Several studies have demonstrated that it is viable to use microcrystalline preparations of water-soluble proteins as...
nmrlearner
Journal club
0
12-01-2010 06:56 PM
[NMR paper] Solution structure and dynamics of integral membrane proteins by NMR: a case study in
Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Related Articles Solution structure and dynamics of integral membrane proteins by NMR: a case study involving the enzyme PagP.
Methods Enzymol. 2005;394:335-50
Authors: Hwang PM, Kay LE
Solution NMR spectroscopy is rapidly becoming an important technique for the study of membrane protein structure and dynamics. NMR experiments on large perdeuterated proteins typically exploit the favorable relaxation properties of backbone amide...
nmrlearner
Journal club
0
11-24-2010 11:14 PM
[NMR paper] Dynamics of trimethoprim bound to dihydrofolate reductase--a deuterium NMR study.
Dynamics of trimethoprim bound to dihydrofolate reductase--a deuterium NMR study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Dynamics of trimethoprim bound to dihydrofolate reductase--a deuterium NMR study.
Solid State Nucl Magn Reson. 1996 Dec;7(3):193-201
Authors: Yang QX, Huang FY, Lin TH, Gelbaum L, Howell EE, Huang TH
We have employed deuterium NMR techniques to determine the dynamics of trimethoprim (TMP) in a binary complex with dihydrofolate reductase...
nmrlearner
Journal club
0
08-22-2010 02:20 PM
[NMR paper] The structure of an integral membrane peptide: a deuterium NMR study of gramicidin.
The structure of an integral membrane peptide: a deuterium NMR study of gramicidin.
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 The structure of an integral membrane peptide: a deuterium NMR study of gramicidin.
Biophys J. 1994 May;66(5):1415-28
Authors: Prosser RS, Daleman SI, Davis JH
Solid state deuterium NMR was employed on oriented multilamellar dispersions...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Dynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramici
Dynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramicidin.
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 Dynamics of an integral membrane peptide: a deuterium NMR relaxation study of gramicidin.
Biophys J. 1994 May;66(5):1429-40
Authors: Prosser RS, Davis JH
Solid state deuterium (2H) NMR inversion-recovery and...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] The structure of an integral membrane peptide: a deuterium NMR study of gramicidin.
The structure of an integral membrane peptide: a deuterium NMR study of gramicidin.
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 The structure of an integral membrane peptide: a deuterium NMR study of gramicidin.
Biophys J. 1994 May;66(5):1415-28
Authors: Prosser RS, Daleman SI, Davis JH
Solid state deuterium NMR was employed on oriented multilamellar dispersions...