[NMR paper] The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR
The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR
The nucleocapsid protein N from SARS-CoV-2 is one of the most highly expressed proteins by the virus and plays a number of important roles in the transcription and assembly of the virion within the infected host cell. It is expected to be characterized by a highly dynamic and heterogeneous structure as can be inferred by bioinformatics analyses as well as from the data available for the homologous protein from SARS-CoV. The two globular domains of the protein (NTD and CTD) have been investigated...
[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...
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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...
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05-16-2020 02:10 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...
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10-21-2014 11:31 PM
[NMR paper] Composition and sequence specific resonance assignments of the heterogeneous N-linked
Composition and sequence specific resonance assignments of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein.
Related Articles Composition and sequence specific resonance assignments of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein.
Biochemistry. 1995 Feb 7;34(5):1622-34
Authors: Wyss DF, Choi JS, Wagner G
CD2, a T cell specific surface adhesion receptor, is critically important for T...
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08-22-2010 03:41 AM
[NMR paper] Sequence-specific resonance assignments of the 1H-NMR spectra of a synthetic, biologi
Sequence-specific resonance assignments of the 1H-NMR spectra of a synthetic, biologically active EIAV Tat protein.
Related Articles Sequence-specific resonance assignments of the 1H-NMR spectra of a synthetic, biologically active EIAV Tat protein.
Biochemistry. 1993 Aug 24;32(33):8439-45
Authors: Willbold D, Krüger U, Frank R, Rosin-Arbesfeld R, Gazit A, Yaniv A, Rösch P
The equine infectious anemia virus (EIAV) trans-activating (Tat) protein is a close homologue of the human immunodeficiency virus (HIV) Tat protein. Both of these proteins...
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08-22-2010 03:01 AM
[NMR paper] Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spect
Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap.
Related Articles Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap.
Biochemistry. 1990 Aug 7;29(31):7191-200
Authors: Wittekind M, Reizer J, Klevit RE
On the basis of an analysis of two-dimensional 1H NMR spectra, the complete sequence-specific 1H NMR assignments are presented for the phosphocarrier protein HPr from the...
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08-21-2010 11:04 PM
[NMR paper] An efficient NMR approach for obtaining sequence-specific resonance assignments of la
An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles An efficient NMR approach for obtaining sequence-specific resonance assignments of larger proteins based on multiple isotopic labeling.
FEBS Lett. 1990 Jun 18;266(1-2):155-8
Authors: Ikura M, Krinks M, Torchia DA, Bax A
By simultaneously incorporating in a protein 13C-carbonyl- and...
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08-21-2010 10:48 PM
[NMR paper] Sequence-specific [1H]NMR resonance assignments and secondary structure identificatio
Sequence-specific NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SW15. A hydrophobic core involving four invariant residues.
Related Articles Sequence-specific NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SW15. A hydrophobic core involving four invariant residues.
FEBS Lett. 1990 Mar 26;262(2):179-84
Authors: Neuhaus D, Nakaseko Y, Nagai K, Klug A
Complete NMR resonance assignments are presented for the second of the three...
The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR
Linear Mode
