Single-Cell NMR? How About Single-Protein NMR? - Corante
Single-Cell NMR? How About Single-Protein NMR? - Corante
Single-Cell NMR? How About Single-Protein NMR? Corante
Two different research teams have reported a completely different way to run NMR experiments, one that looks like it could take the resolution down to cellular (or even large protein) levels. These two papers in Science have the details (and there's an ...
Single-shot NMR measurement of protein unfolding landscapes
Single-shot NMR measurement of protein unfolding landscapes
June 2012
Publication year: 2012
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, Volume 1824, Issue 6</br>
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The transient unfolding events from the native state of a protein towards higher energy states can be closely investigated by studying the process of hydrogen exchange. Here, we present BLUU-Tramp (Biophysics Laboratory University of Udine—Temperature ramp), a new method to measure the rates for the exchange process and the underlying equilibrium thermodynamic parameters, using...
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Neurotransmission is controlled by a single protein - R & D Magazine
Neurotransmission is controlled by a single protein - R & D Magazine
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Neurotransmission is controlled by a single protein
R & D Magazine
The alpha 2 delta protein is the target of this drug and the new work suggests an .... of a new 0.75-mm solid state nuclear magnetic resonance (NMR) probe.
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06-13-2012 11:34 AM
[NMR paper] NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: c
NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: contribution of a beta hairpin to RNA binding.
Related Articles NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: contribution of a beta hairpin to RNA binding.
Biochemistry. 2005 Mar 15;44(10):3708-17
Authors: Volpon L, D'Orso I, Young CR, Frasch AC, Gehring K
TcUBP1 is a trypanosome cytoplasmic RNA-binding protein containing a single, conserved RNA-recognition motif (RRM) domain involved in selective destabilization of U-rich...
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11-24-2010 11:14 PM
[NMR paper] NMR structures of three single-residue variants of the human prion protein.
NMR structures of three single-residue variants of the human prion protein.
Related Articles NMR structures of three single-residue variants of the human prion protein.
Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8340-5
Authors: Calzolai L, Lysek DA, Guntert P, von Schroetter C, Riek R, Zahn R, Wüthrich K
The NMR structures of three single-amino acid variants of the C-terminal domain of the human prion protein, hPrP(121-230), are presented. In hPrP(M166V) and hPrP(R220K) the substitution is with the corresponding residue in murine PrP, and in...
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11-19-2010 08:29 PM
[NMR paper] Interactions of a didomain fragment of the Drosophila sex-lethal protein with single-
Interactions of a didomain fragment of the Drosophila sex-lethal protein with single-stranded uridine-rich oligoribonucleotides derived from the transformer and Sex-lethal messenger RNA precursors: NMR with residue-selective uridine substitutions.
Related Articles Interactions of a didomain fragment of the Drosophila sex-lethal protein with single-stranded uridine-rich oligoribonucleotides derived from the transformer and Sex-lethal messenger RNA precursors: NMR with residue-selective uridine substitutions.
J Biomol NMR. 2000 Jun;17(2):153-65
Authors: Kim...
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[NMR paper] NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer
NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
Related Articles NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer beta-sheet.
J Biomol NMR. 1998 May;11(4):407-14
Authors: Pham TN, Koide S
The crystal structure of outer surface protein A (OspA) from Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and it is solvent-exposed on both faces, which...
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11-17-2010 11:06 PM
[NMR paper] Interaction of myelin basic protein with single bilayers on a solid support: an NMR,
Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study.
Related Articles Interaction of myelin basic protein with single bilayers on a solid support: an NMR, DSC and polarized infrared ATR study.
Biochim Biophys Acta. 1993 Sep 19;1151(2):127-36
Authors: Reinl HM, Bayerl TM
The interaction of myelin basic protein (MBP) with single bilayers on a solid support (planar and spherical support) is studied by deuterium nuclear magnetic resonance (2H-NMR), differential scanning...
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[NMR paper] Representing an ensemble of NMR-derived protein structures by a single structure.
Representing an ensemble of NMR-derived protein structures by a single structure.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Representing an ensemble of NMR-derived protein structures by a single structure.
Protein Sci. 1993 Jun;2(6):936-44
Authors: Sutcliffe MJ
The usefulness of representing an ensemble of...