[NMR paper] Unique epitope-antibody interactions in the intrinsically disordered proteoglycan-like domain of human carbonic anhydrase IX defined by high-resolution NMR combined with yeast surface display
Unique epitope-antibody interactions in the intrinsically disordered proteoglycan-like domain of human carbonic anhydrase IX defined by high-resolution NMR combined with yeast surface display
Carbonic anhydrase (CA)-IX is an extracellular enzyme that is essential in the adaptation of tumor cells to their increasingly more hypoxic and acidic microenvironment. Within the family of carbonic anhydrases, CA-IX is unique in that it is the only CA with an N-terminal intrinsically disordered region (IDR) containing a proteoglycan (PG)-like domain. This PG-like IDR has been described to be instrumental in CA-IX's enzyme activity, as well as tumor cell motility and invasion. We have...
[NMR paper] NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
NMR Provides Unique Insight into the Functional Dynamics and Interactions of Intrinsically Disordered Proteins
Intrinsically disordered proteins are ubiquitous throughout all known proteomes, playing essential roles in all aspects of cellular and extracellular biochemistry. To understand their function, it is necessary to determine their structural and dynamic behavior and to describe the physical chemistry of their interaction trajectories. Nuclear magnetic resonance is perfectly adapted to this task, providing ensemble averaged structural and dynamic parameters that report on each...
nmrlearner
Journal club
0
04-22-2022 03:01 AM
[NMR paper] Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.
Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.
Related Articles Ensemble description of the intrinsically disordered N-terminal domain of the Nipah virus P/V protein from combined NMR and SAXS.
Sci Rep. 2020 Nov 11;10(1):19574
Authors: Schiavina M, Salladini E, Murrali MG, Tria G, Felli IC, Pierattelli R, Longhi S
Abstract
Using SAXS and NMR spectroscopy, we herein provide a high-resolution description of the intrinsically disordered N-terminal...
nmrlearner
Journal club
0
11-13-2020 04:07 PM
[NMR paper] NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using (15) N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations.
NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using (15) N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations.
NMR Studies of Active-Site Properties of Human Carbonic Anhydrase II by using (15) N-Labeled 4-Methylimidazole as a Local Probe and Histidine Hydrogen-Bond Correlations.
Chemistry. 2014 Dec 17;
Authors: Shenderovich IG, Lesnichin SB, Tu C, Silverman DN, Tolstoy PM, Denisov GS, Limbach H
Abstract
By using a combination of liquid and solid-state NMR spectroscopy,...
nmrlearner
Journal club
0
12-19-2014 11:42 AM
[NMR paper] Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Related Articles Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Chembiochem. 2013 Jun 6;
Authors: Amata I, Maffei M, Igea A, Gay M, Vilaseca M, Nebreda AR, Pons M
Abstract
Intrinsically disordered regions (IDRs) are preferred sites for post-translational modifications essential for regulating protein function. The enhanced local...
nmrlearner
Journal club
0
06-08-2013 02:18 PM
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
Abstract Four novel 5D (HACA(N)CONH, HNCOCACB, (HACA)CON(CA)CONH, (H)NCO(NCA)CONH), and one 6D ((H)NCO(N)CACONH) NMR pulse sequences are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in indirectly detected dimensions. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel pulse sequences were successfully tested using δ subunit (20 kDa) of Bacillus subtilis RNA polymerase...
nmrlearner
Journal club
0
02-21-2012 03:40 AM
[NMR paper] Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NM
Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study.
Related Articles Water-protein interactions in the molten-globule state of carbonic anhydrase b: an NMR spin-diffusion study.
Protein Sci. 2000 Aug;9(8):1540-7
Authors: Kutyshenko VP, Cortijo M
We have used the homonuclear Overhauser effect (NOE) to characterize a model protein: carbonic anhydrase B. We have obtained NOE difference spectra for this protein, centering the on-resonance signals either at the methyl-proton or at the...
nmrlearner
Journal club
0
11-19-2010 08:29 PM
[NMR paper] Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by
Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.
Related Articles Sequential assignment of 1H, 13C and 15N resonances of human carbonic anhydrase I by triple-resonance NMR techniques and extensive amino acid-specific 15N-labeling.
J Biomol NMR. 1996 Dec;8(4):417-28
Authors: Sethson I, Edlund U, Holak TA, Ross A, Jonsson BH
The backbone NMR resonances of human carbonic anhydrase I (HCA I) have been assigned. This protein is one of...
nmrlearner
Journal club
0
08-22-2010 02:20 PM
[NMR paper] Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium e
Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Denatured states of human carbonic anhydrase II: an NMR study of hydrogen/deuterium exchange at tryptophan-indole-H(N) sites.
FEBS Lett. 1999 Feb 26;445(2-3):361-5
Authors: Jonasson P, Kjellsson A, Sethson I, Jonsson BH
Hydrogen/deuterium (H/D) exchange measurements in low and moderate...
Unique epitope-antibody interactions in the intrinsically disordered proteoglycan-like domain of human carbonic anhydrase IX defined by high-resolution NMR combined with yeast surface display
Linear Mode
