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30-or nmr spectroscopy reveals unexpected structural variation at the protein-protein interface in mhc class i molecules
30-OR NMR SPECTROSCOPY REVEALS UNEXPECTED STRUCTURAL VARIATION AT THE PROTEIN-PROTEIN INTERFACE IN MHC CLASS I MOLECULES
Publication date: November 2013
Source:Human Immunology, Volume 74, Supplement</br>
Author(s): Andreas Ziegler , Monika Beerbaum , Martin Ballaschk , Natalja Erdmann , Christina Schnick , Anne Diehl , Barbara Uchanska-Ziegler , Peter Schmieder</br>
Aim ?2-microglobulin (?2m) is a small, monomorphic protein non-covalently bound to the heavy chain (HC) in polymorphic major histocompatibility complex (MHC) class I molecules. Given the high...
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10-17-2013 04:38 AM
[NMR paper] NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.
NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.
NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.
J Biomol NMR. 2013 Sep 5;
Authors: Beerbaum M, Ballaschk M, Erdmann N, Schnick C, Diehl A, Uchanska-Ziegler B, Ziegler A, Schmieder P
Abstract
?2-Microglobulin (?2m) is a small, monomorphic protein non-covalently bound to the heavy chain (HC) in polymorphic major histocompatibility complex (MHC) class I...
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09-06-2013 06:52 PM
[NMR images] Protein NMR Spectroscopy - Buch portofrei bei Weltbild.de kaufen
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06-27-2013 02:10 PM
Comprehensive Determination of Protein Tyrosine pKa Values for Photoactive Yellow Protein Using Indirect 13C NMR Spectroscopy
Comprehensive Determination of Protein Tyrosine pKa Values for Photoactive Yellow Protein Using Indirect 13C NMR Spectroscopy
8 February 2012
Publication year: 2012
Source:Biophysical Journal, Volume 102, Issue 3</br>
</br>
Upon blue-light irradiation, the bacterium Halorhodospira halophila is able to modulate the activity of its flagellar motor and thereby evade potentially harmful UV radiation. The 14*kDa soluble cytosolic photoactive yellow protein (PYP) is believed to be the primary mediator of this photophobic response, and yields a UV/Vis absorption spectrum that...
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02-03-2013 10:13 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these interactions...
nmrlearner
Journal club
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09-30-2011 06:00 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these...
nmrlearner
Journal club
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09-30-2011 05:59 AM
[NMR paper] Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Related Articles Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
J Biomol NMR. 2005 Jul;32(3):195-207
Authors: Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for...
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12-01-2010 06:56 PM
[NMR paper] Facile detection of protein-protein interactions by one-dimensional NMR spectroscopy.
Facile detection of protein-protein interactions by one-dimensional NMR spectroscopy.
Related Articles Facile detection of protein-protein interactions by one-dimensional NMR spectroscopy.
Biochemistry. 2003 Mar 18;42(10):2774-80
Authors: Araç D, Murphy T, Rizo J
Two methods for detecting protein-protein interactions in solution using one-dimensional (1D) NMR spectroscopy are described. Both methods rely on measurement of the intensity of the strongest methyl resonance (SMR), which for most proteins is observed at 0.8-0.9 ppm. The severe...
Protein NMR Spectroscopy Buch portofrei bei Weltbild.de bestellen
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