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[NMR paper] Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.
Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.
Examining weak protein-protein interactions in start codon recognition via NMR spectroscopy.
FEBS J. 2013 Nov 30;
Authors: Luna RE, Akabayov SR, Ziarek JJ, Wagner G
Abstract
Weak protein-protein interactions are critical in numerous biological processes. Unfortunately, they are difficult to characterize due to the high concentrations required for the production and detection of the complex population. The inherent sensitivity of NMR...
[NMR paper] Recent advances in protein NMR spectroscopy and their implications in protein therapeutics research.
Recent advances in protein NMR spectroscopy and their implications in protein therapeutics research.
Related Articles Recent advances in protein NMR spectroscopy and their implications in protein therapeutics research.
Anal Bioanal Chem. 2013 Dec 6;
Authors: Wang G, Zhang ZT, Jiang B, Zhang X, Li C, Liu M
Abstract
Nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography are the two main methods for protein three-dimensional structure determination at atomic resolution. According to the protein structures deposited in the...
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12-07-2013 01:00 PM
[NMR images] Protein NMR Spectroscopy Buch portofrei bei Weltbild.de bestellen
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12/11/2013 3:33:55 AM GMT
Protein NMR Spectroscopy Buch portofrei bei Weltbild.de bestellen
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11-12-2013 03:33 AM
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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27/06/2013 2:11:11 PM GMT
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...
Protein NMR Spectroscopy Buch portofrei bei Weltbild.de bestellen
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