[NMR paper] Recrystallized S-layer protein of a probiotic propionibacterium: structural and nanomechanical changes upon temperature or pH shifts probed by solid-state NMR and AFM.
Recrystallized S-layer protein of a probiotic propionibacterium: structural and nanomechanical changes upon temperature or pH shifts probed by solid-state NMR and AFM.
Recrystallized S-layer protein of a probiotic propionibacterium: structural and nanomechanical changes upon temperature or pH shifts probed by solid-state NMR and AFM.
Langmuir. 2014 Dec 5;
Authors: De Sa Peixoto P, Roiland C, Thomas D, Briard-Bion V, Le Guellec R, Parayre S, Deutsch SM, Jan G, Guyomarc'h F
Abstract
Surface protein layers (S layers) are common constituents of the bacterial cell wall and originate from the assembly of strain-dependent surface layer proteins (Slps). These proteins are thought to play important roles in the bacteria's biology and to have very promising technological applications as biomaterials or as part of cell-host cross-talk in probiotic mechanism. The SlpA from Propionibacterium freudenreichii PFCIRM 118 strain was isolated and recrystallized to investigate organization and assembly of the protein using atomic force microscopy and solid-state 1H and 13C-nuclear magnetic resonance. SlpA was found to form hexagonal p1 monolayer lattices where the protein exhibited high proportions of disordered regions and of bound water. The lattice structure was maintained, but softened, upon mild heating or acidification, probably in relation with the increasing mobilities of the disordered protein regions. These results gave structural insights on the mobile protein regions exposed by S layer films, upon physiologically relevant changes of their environmental conditions.
PMID: 25479375 [PubMed - as supplied by publisher]
[NMR paper] Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR.
Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR.
Related Articles Conformational dynamics of a seven transmembrane helical protein Anabaena Sensory Rhodopsin probed by solid-state NMR.
J Am Chem Soc. 2014 Jan 27;
Authors: Good DB, Wang S, Ward ME, Struppe JO, Brown LS, Lewandowski JR, Ladizhansky V
Abstract
The ability to detect and characterize molecular motions represents one of the unique strengths of Nuclear Magnetic Resonance (NMR) spectroscopy. In this study we...
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01-29-2014 02:01 PM
[NMR paper] Protein-RNA Interfaces Probed by (1) H-Detected MAS Solid-State NMR Spectroscopy.
Protein-RNA Interfaces Probed by (1) H-Detected MAS Solid-State NMR Spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Protein-RNA Interfaces Probed by (1) H-Detected MAS Solid-State NMR Spectroscopy.
Angew Chem Int Ed Engl. 2013 Jan 18;
Authors: Asami S, Rakwalska-Bange M, Carlomagno T, Reif B
Abstract
Both protonated and deuterated samples were employed in the study of the L7Ae box C/D RNA complex by (1) H-detected...
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02-03-2013 10:19 AM
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy
Jonathan J. Helmus, Krystyna Surewicz, Marcin I. Apostol, Witold K. Surewicz and Christopher P. Jaroniec
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206469q/aop/images/medium/ja-2011-06469q_0003.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206469q
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/e9F1wuu5168
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08-16-2011 03:17 AM
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR
Abstract X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100 K. Protein dynamics are poorly understood below the freezing point of water and down to liquid nitrogen temperatures. Therefore, we investigate the α-spectrin SH3 domain by magic angle spinning (MAS) solid state NMR (ssNMR) at various temperatures while cooling slowly. Cooling down...
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08-13-2011 02:47 AM
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy.
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy.
Intermolecular Alignment in Y145Stop Human Prion Protein Amyloid Fibrils Probed by Solid-State NMR Spectroscopy.
J Am Chem Soc. 2011 Aug 10;
Authors: Helmus JJ, Surewicz K, Apostol MI, Surewicz WK, Jaroniec CP
The Y145Stop mutant of human prion protein, huPrP23-144, has been linked to PrP cerebral amyloid angiopathy, an inherited amyloid disease, and also serves as a valuable in vitro model for investigating the molecular basis of...
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08-11-2011 12:32 PM
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
J Biomol NMR. 2011 Aug 9;
Authors: Linden AH, Franks WT, Akbey U, Lange S, van Rossum BJ, Oschkinat H
X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100*K. Protein dynamics are poorly understood...
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08-10-2011 12:30 PM
[NMR paper] Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state
Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state NMR spectroscopy.
Related Articles Membrane protein topology probed by (1)H spin diffusion from lipids using solid-state NMR spectroscopy.
J Am Chem Soc. 2002 Feb 6;124(5):874-83
Authors: Huster D, Yao X, Hong M
We describe a two-dimensional solid-state NMR technique to investigate membrane protein topology under magic-angle spinning conditions. The experiment detects the rate of (1)H spin diffusion from the mobile lipids to the rigid protein. While spin...
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11-24-2010 08:49 PM
Supramolecular Interactions Probed by (13)C-(13)C Solid-State NMR Spectroscopy.
Supramolecular Interactions Probed by (13)C-(13)C Solid-State NMR Spectroscopy.
Related Articles Supramolecular Interactions Probed by (13)C-(13)C Solid-State NMR Spectroscopy.
J Am Chem Soc. 2010 Oct 8;
Authors: Loquet A, Giller K, Becker S, Lange A
We present a robust solid-state NMR approach for the accurate determination of molecular interfaces in insoluble and noncrystalline protein-protein complexes. The method relies on the measurement of intermolecular (13)C-(13)C distances in mixtures of glucose- and glucose-labeled proteins. We have...