[NMR paper] ?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
?-Helical architecture of cytoskeletal bactofilin filaments revealed by solid-state NMR.
Proc Natl Acad Sci U S A. 2014 Dec 30;
Authors: Vasa S, Lin L, Shi C, Habenstein B, Riedel D, Kühn J, Thanbichler M, Lange A
Abstract
Bactofilins are a widespread class of bacterial filament-forming proteins, which serve as cytoskeletal scaffolds in various cellular pathways. They are characterized by a conserved architecture, featuring a central...
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Interactions of gemini surfactants with two model proteins: NMR, CD, and fluorescence spectroscopies
Interactions of gemini surfactants with two model proteins: NMR, CD, and fluorescence spectroscopies
1 March 2012
Publication year: 2012
Source:Journal of Colloid and Interface Science, Volume 369, Issue 1</br>
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Gemini surfactants have two polar head groups and two hydrocarbon tails. Compared with conventional surfactants, geminis have much lower (?M vs. mM) critical micelle concentrations and possess slower (ms vs. ?s) monomer ? micelle kinetics. The structure of the gemini surfactants studied is ·2Br- where s =4, 5, or 6. Our objective is to reveal the effect...
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Solution NMR studies of polytopic ?-helical membrane proteins.
Solution NMR studies of polytopic ?-helical membrane proteins.
Solution NMR studies of polytopic ?-helical membrane proteins.
Curr Opin Struct Biol. 2011 Jul 18;
Authors: Nietlispach D, Gautier A
NMR spectroscopy has established itself as one of the main techniques for the structural study of integral membrane proteins. Remarkably, over the last few years, substantial progress has been achieved in the structure determination of increasingly complex polytopical ?-helical membrane proteins, with their size approaching ~100kDa. Such advances are the...
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[NMR paper] Metal ion binding to calmodulin: NMR and fluorescence studies.
Metal ion binding to calmodulin: NMR and fluorescence studies.
Related Articles Metal ion binding to calmodulin: NMR and fluorescence studies.
Biometals. 1998 Sep;11(3):213-22
Authors: Ouyang H, Vogel HJ
Calmodulin is an important second messenger protein which is involved in a large variety of cellular pathways. Calmodulin is sensitive to fluctuations in the intracellular Ca2+ levels and is activated by the binding of four Ca2+ ions. In spite of the important role it plays in signal transduction pathways, it shows a surprisingly broad...
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[NMR paper] On choosing a detergent for solution NMR studies of membrane proteins.
On choosing a detergent for solution NMR studies of membrane proteins.
Related Articles On choosing a detergent for solution NMR studies of membrane proteins.
J Biomol NMR. 1998 May;11(4):381-6
Authors: Vinogradova O, Sönnichsen F, Sanders CR
Translational diffusion coefficients and catalytic activities were measured for the integral membrane protein diacylglycerol kinase (DAGK) in a variety of types of detergent micelles. Despite the structural diversity of the detergents examined, the translational diffusion coefficients observed for DAGK...
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[NMR paper] 1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lip
1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lipid transfer protein. Global fold of the complex.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lipid transfer protein. Global fold of the complex.
FEBS Lett. 1997 Oct 20;416(2):130-4
Authors: Sodano P, Caille A, Sy D, de Person G, Marion D, Ptak M
Plant non-specific lipid transfer proteins (LTPs) are...
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[NMR paper] Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvi
Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein.
Related Articles Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein.
Biochemistry. 1994 Jan 11;33(1):65-73
Authors: Yamasaki K, Shirouzu M, Muto Y, Fujita-Yoshigaki J, Koide H, Ito Y, Kawai G, Hattori S, Yokoyama S, Nishimura S
The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
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[NMR paper] Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvi
Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein.
Related Articles Site-directed mutagenesis, fluorescence, and two-dimensional NMR studies on microenvironments of effector region aromatic residues of human c-Ha-Ras protein.
Biochemistry. 1994 Jan 11;33(1):65-73
Authors: Yamasaki K, Shirouzu M, Muto Y, Fujita-Yoshigaki J, Koide H, Ito Y, Kawai G, Hattori S, Yokoyama S, Nishimura S
The Tyr residues in positions 32 and 40 of human c-Ha-Ras...
Fluorescence Microscopy and Solution NMR Studies of Cytoskeletal Proteins from Tetrahymena
Linear Mode
