Related ArticlesSecondary structure, dynamics, and architecture of the p7 membrane protein from hepatitis c virus by NMR spectroscopy.
Biochim Biophys Acta. 2010 Aug 18;
Authors: Cook GA, Opella SJ
P7 is a small membrane protein that is essential for the infectivity of hepatitis C virus. Solution-state NMR experiments on p7 in DHPC micelles, including hydrogen/deuterium exchange, paramagnetic relaxation enhancement and bicelle 'q-titration'; demonstrate that the protein has a range of dynamic properties and distinct structural segments. These data along with residual dipolar couplings yield a secondary structure model of p7. We were able to confirm previous proposals that the protein has two transmembrane segments with a short interhelical loop containing the two basic residues K33 and R35. The 63-amino acid protein has a remarkably complex structure made up of 7 identifiable sections, four of which are helical segments with different tilt angles and dynamics. A solid-state NMR two-dimensional separated local field spectrum of p7 aligned in phospholipid bilayers provided the tilt angles of two of these segments. A preliminary structural model of p7 derived from these NMR data is presented.
PMID: 20727850 [PubMed - as supplied by publisher]
[NMR paper] Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
Related Articles Determination of membrane protein structure and dynamics by magic-angle-spinning solid-state NMR spectroscopy.
J Am Chem Soc. 2005 Sep 21;127(37):12965-74
Authors: Andronesi OC, Becker S, Seidel K, Heise H, Young HS, Baldus M
It is shown that molecular structure and dynamics of a uniformly labeled membrane protein can be studied under magic-angle-spinning conditions. For this purpose, dipolar recoupling experiments...
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[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...
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[NMR paper] NMR structure of Mistic, a membrane-integrating protein for membrane protein expressi
NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.
Related Articles NMR structure of Mistic, a membrane-integrating protein for membrane protein expression.
Science. 2005 Feb 25;307(5713):1317-21
Authors: Roosild TP, Greenwald J, Vega M, Castronovo S, Riek R, Choe S
Although structure determination of soluble proteins has become routine, our understanding of membrane proteins has been limited by experimental bottlenecks in obtaining both sufficient yields of protein and ordered crystals. Mistic is an...
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[NMR paper] Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza
Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
Related Articles Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR.
FEBS Lett. 2003 Nov 27;555(1):139-43
Authors: Tamm LK, Abildgaard F, Arora A, Blad H, Bushweller JH
Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles...
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[NMR paper] Membrane structure and dynamics as viewed by solid-state NMR spectroscopy.
Membrane structure and dynamics as viewed by solid-state NMR spectroscopy.
Related Articles Membrane structure and dynamics as viewed by solid-state NMR spectroscopy.
Biophys Chem. 1997 Oct;68(1-3):233-41
Authors: Auger M
The purpose of the present study is the investigation of the structure and dynamics of biological membranes using solid-state nuclear magnetic resonance (NMR) spectroscopy. Two approaches are used in our laboratory. The first involves the measurement of high-resolution 13C and 1H spectra obtained by the magic angle spinning...
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[NMR paper] Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein u
Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.
Related Articles Assignments, secondary structure, global fold, and dynamics of chemotaxis Y protein using three- and four-dimensional heteronuclear (13C,15N) NMR spectroscopy.
Biochemistry. 1994 Sep 6;33(35):10731-42
Authors: Moy FJ, Lowry DF, Matsumura P, Dahlquist FW, Krywko JE, Domaille PJ
NMR spectroscopy has been used to study recombinant Escherichia coli CheY, a 128-residue...
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[NMR paper] NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat pr
NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Related Articles NMR studies of the structure and dynamics of membrane-bound bacteriophage Pf1 coat protein.
Science. 1991 May 31;252(5010):1303-5
Authors: Shon KJ, Kim Y, Colnago LA, Opella SJ
Filamentous bacteriophage coat protein undergoes a remarkable structural transition during the viral assembly process as it is transferred from the membrane environment of the cell, where it spans the phospholipid bilayer, to the newly extruded virus particles....
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Simultaneous Structure and Dynamics of a Membrane Protein using REDCRAFT: Membrane-bo
Simultaneous Structure and Dynamics of a Membrane Protein using REDCRAFT: Membrane-bound form of Pf1 Coat Protein
Publication year: 2010
Source: Journal of Magnetic Resonance, In Press, Accepted Manuscript, Available online 30 July 2010</br>
Paul, Shealy , Mikhail, Simin , Sang Ho, Park , Stanley J., Opella , Homayoun, Valafar</br>
A strategy for simultaneous study of the structure and internal dynamics of a membrane protein is described using the REDCRAFT algorithm. The membrane-bound form of the Pf1 major coat protein (mbPf1) was used as an example. First, synthetic data is...
Secondary structure, dynamics, and architecture of the p7 membrane protein from hepat
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