[NMR paper] NMR mapping of the highly flexible regions of 13C/15N-labeled antibody TTAC-0001-Fab.
NMR mapping of the highly flexible regions of 13C/15N-labeled antibody TTAC-0001-Fab.
Related Articles NMR mapping of the highly flexible regions of 13C/15N-labeled antibody TTAC-0001-Fab.
J Biomol NMR. 2020 May 15;:
Authors: Cha S, Lee WS, Choi J, Jeong JG, Nam JR, Kim J, Kim HN, Lee JH, Yoo JS, Ryu KS
Abstract
Monoclonal antibody (mAb) drugs are clinically important for the treatment of various diseases. TTAC-0001 is under development as a new anti-cancer antibody drug targeting VEGFR-2. As the less severe toxicity of TTAC-0001...
nmrlearner
Journal club
0
05-18-2020 09:18 PM
NMR mapping of the highly flexible regions of 13 C/ 15 N-labeled antibody TTAC-0001-Fab
NMR mapping of the highly flexible regions of 13 C/ 15 N-labeled antibody TTAC-0001-Fab
Abstract
Monoclonal antibody (mAb) drugs are clinically important for the treatment of various diseases. TTAC-0001 is under development as a new anti-cancer antibody drug targeting VEGFR-2. As the less severe toxicity of TTAC-0001 compared to Bevacizumab, likely due to the decreased in vivo half-life, seems to be related to its structural flexibility, it is important to map the exact flexible regions. Although the 13C/15N-labeled protein is required for NMR...
nmrlearner
Journal club
0
05-16-2020 02:10 AM
DynamicDescriptions of Highly Flexible Moleculesfrom NMR Dipolar Couplings: Physical Basis and Limitations
DynamicDescriptions of Highly Flexible Moleculesfrom NMR Dipolar Couplings: Physical Basis and Limitations
Nicola Salvi, Loi?c Salmon and Martin Blackledge
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.7b01566/20170329/images/medium/ja-2017-01566y_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.7b01566
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/usX6DdNyVP4
nmrlearner
Journal club
0
03-30-2017 05:44 AM
â??CON-CONâ?? assignment strategy for highly flexible intrinsically disordered proteins
â??CON-CONâ?? assignment strategy for highly flexible intrinsically disordered proteins
Abstract
Intrinsically disordered proteins (IDPs) are a class of highly flexible proteins whose characterization by NMR spectroscopy is complicated by severe spectral overlaps. The development of experiments designed to facilitate the sequence-specific assignment procedure is thus very important to improve the tools for the characterization of IDPs and thus to be able to focus on IDPs of increasing size and complexity. Here, we present and describe the...
nmrlearner
Journal club
0
10-21-2014 11:31 PM
[NMR paper] Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.
Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.
Related Articles Determination of the individual roles of the linker residues in the interdomain motions of calmodulin using NMR chemical shifts.
J Mol Biol. 2014 Feb 11;
Authors: Kukic P, Camilloni C, Cavalli A, Vendruscolo M
Abstract
Many protein molecules are formed by two or more domains whose structures and dynamics are closely related to their biological functions. It is thus important to develop methods to...
nmrlearner
Journal club
0
02-19-2014 12:07 AM
Interdomain Dynamics Explored by Paramagnetic NMR
Interdomain Dynamics Explored by Paramagnetic NMR
Luigi Russo, Mitcheell Maestre-Martinez, Sebastian Wolff, Stefan Becker and Christian Griesinger
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja408143f/aop/images/medium/ja-2013-08143f_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja408143f
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ShdDw1zwpdY