[NMR paper] A combination of 19F NMR and surface plasmon resonance for site-specific hit selection and validation of fragment molecules that bind to the ATP-binding site of a kinase.
A combination of 19F NMR and surface plasmon resonance for site-specific hit selection and validation of fragment molecules that bind to the ATP-binding site of a kinase.
A combination of 19F NMR and surface plasmon resonance for site-specific hit selection and validation of fragment molecules that bind to the ATP-binding site of a kinase.
Bioorg Med Chem. 2018 Feb 22;:
Authors: Nagatoishi S, Yamaguchi S, Katoh E, Kajita K, Yokotagawa T, Kanai S, Furuya T, Tsumoto K
Abstract
19F NMR has recently emerged as an efficient,...
nmrlearner
Journal club
0
03-08-2018 01:24 PM
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...
nmrlearner
Journal club
0
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...
nmrlearner
Journal club
0
09-06-2013 06:52 PM
[NMR paper] Solid-State (13)C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein.
Solid-State (13)C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein.
Related Articles Solid-State (13)C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein.
J Mol Biol. 2013 Apr 11;
Authors: Leftin A, Job C, Beyer K, Brown MF
Abstract
Misfolding and aggregation of the intrinsically disordered protein ?-Synuclein (?S) in Lewy body plaques is a characteristic marker of late-stage Parkinson's disease. It is...
nmrlearner
Journal club
0
04-16-2013 07:46 PM
Solid-State 13C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein
Solid-State 13C NMR Reveals Annealing of Raft-Like Membranes Containing Cholesterol by the Intrinsically Disordered Protein ?-Synuclein
Publication date: Available online 11 April 2013
Source:Journal of Molecular Biology</br>
Author(s): Avigdor Leftin , Constantin Job , Klaus Beyer , Michael F. Brown</br>
Misfolding and aggregation of the intrinsically disordered protein ?-Synuclein (?S) in Lewy body plaques is a characteristic marker of late-stage Parkinson’s disease. It is well established that membrane binding is initiated at the N-terminus of the protein and...
NMR Spectroscopy Reveals How Cholesterol Molecules Bind to a Flu Protein - SciTechDaily
Linear Mode
